query: where are atp synthase complexes located in a plant cell

pos: ATP synthase or the plasma membrane in bacteria. During photosynthesis in plants, ATP is synthesized by ATP synthase using a proton gradient created in the thylakoid lumen through the thylakoid membrane and into the chloroplast stroma. ATP synthase consists of two main subunits, F and F, which has a rotational motor mechanism allowing for ATP production. Because of its rotating subunit, ATP synthase is a molecular machine. The F fraction derives its name from the term "Fraction 1" and F (written as a subscript letter "o", not "zero") derives its name from being the binding fraction for oligomycin, a type of naturally-derived

pos: Light-dependent reactions Light-dependent reactions In photosynthesis, the light-dependent reactions take place on the thylakoid membranes. The inside of the thylakoid membrane is called the lumen, and outside the thylakoid membrane is the stroma, where the light-independent reactions take place. The thylakoid membrane contains some integral membrane protein complexes that catalyze the light reactions. There are four major protein complexes in the thylakoid membrane: Photosystem II (PSII), Cytochrome b6f complex, Photosystem I (PSI), and ATP synthase. These four complexes work together to ultimately create the products ATP and NADPH. The four photosystems absorb light energy through pigments—primarily the chlorophylls, which are responsible for

pos: Light-dependent reactions place only in the presence of light. This led later to the discovery of photosystems I and II. Light-dependent reactions In photosynthesis, the light-dependent reactions take place on the thylakoid membranes. The inside of the thylakoid membrane is called the lumen, and outside the thylakoid membrane is the stroma, where the light-independent reactions take place. The thylakoid membrane contains some integral membrane protein complexes that catalyze the light reactions. There are four major protein complexes in the thylakoid membrane: Photosystem II (PSII), Cytochrome b6f complex, Photosystem I (PSI), and ATP synthase. These four complexes work together to ultimately create the

pos: Thylakoid with known functions, 42% are involved in photosynthesis. The next largest functional groups include proteins involved in protein targeting, processing and folding with 11%, oxidative stress response (9%) and translation (8%). Thylakoid membranes contain integral membrane proteins which play an important role in light harvesting and the light-dependent reactions of photosynthesis. There are four major protein complexes in the thylakoid membrane: Photosystem II is located mostly in the grana thylakoids, whereas photosystem I and ATP synthase are mostly located in the stroma thylakoids and the outer layers of grana. The cytochrome b6f complex is distributed evenly throughout thylakoid membranes. Due

pos: ATP synthase is integrated into thylakoid membrane; the CF-part sticks into stroma, where dark reactions of photosynthesis (also called the light-independent reactions or the Calvin cycle) and ATP synthesis take place. The overall structure and the catalytic mechanism of the chloroplast ATP synthase are almost the same as those of the bacterial enzyme. However, in chloroplasts, the proton motive force is generated not by respiratory electron transport chain but by primary photosynthetic proteins. The ATP synthase isolated from bovine ("Bos taurus") heart mitochondria is, in terms of biochemistry and structure, the best-characterized ATP synthase. Beef heart is used as a source for

pos: Nucleoside triphosphate both cellular respiration and photosynthesis by ATP synthase. ATP synthase couples the synthesis of ATP from ADP and phosphate with an electrochemical gradient generated by the pumping of protons through either the inner mitochondrial membrane (cellular respiration) or the thylakoid membrane (photosynthesis). This electrochemical gradient is necessary because the formation of ATP is energetically unfavourable. The hydrolysis of ATP to ADP and Pi proceeds as follows: This reaction is energetically favourable and releases 30.5 kJ/mol of energy. In the cell, this reaction is often coupled with unfavourable reactions to provide the energy for them to proceed. GTP is occasionally used

pos: ATP synthase antibiotic that is able to inhibit the F unit of ATP synthase. These functional regions consist of different protein subunits — refer to tables. This enzyme is used in synthesis of ATP through aerobic respiration. Located within the thylakoid membrane and the inner mitochondrial membrane, ATP synthase consists of two regions F and F. F causes rotation of F and is made of c-ring and subunits a, b, d, F6. F is made of formula_1 subunits. F has a water-soluble part that can hydrolyze ATP. F on the other hand has mainly hydrophobic regions. F F creates a pathway for

pos: Hydrogen ion are derived." Hydrogen anions are formed when additional electrons are acquired: Hydrogen ions drive ATP synthase in photosynthesis. This happens when hydrogen ions get pushed across the membrane creating a high concentration inside the thylakoid membrane and a low concentration in the cytoplasm. However, because of osmosis, the H will force itself out of the membrane through ATP synthase. Using their kinetic energy to escape, the protons will spin the ATP synthase which in turn will create ATP. This happens in cellular respiration as well though the concentrated membrane will instead be the inner membrane of the mitochondria. Hydrogen ions

pos: ATP synthase or the plasma membrane in bacteria. During photosynthesis in plants, ATP is synthesized by ATP synthase using a proton gradient created in the thylakoid lumen through the thylakoid membrane and into the chloroplast stroma. ATP synthase consists of two main subunits, F and F, which has a rotational motor mechanism allowing for ATP production. Because of its rotating subunit, ATP synthase is a molecular machine. The F fraction derives its name from the term "Fraction 1" and F (written as a subscript letter "o", not "zero") derives its name from being the binding fraction for oligomycin, a type of naturally-derived

pos: Chloroplast circular disks about 300–600 nanometers in diameter. Stromal thylakoids are helicoid sheets that spiral around grana. The flat tops and bottoms of granal thylakoids contain only the relatively flat photosystem II protein complex. This allows them to stack tightly, forming grana with many layers of tightly appressed membrane, called granal membrane, increasing stability and surface area for light capture. In contrast, photosystem I and ATP synthase are large protein complexes which jut out into the stroma. They can't fit in the appressed granal membranes, and so are found in the stromal thylakoid membrane—the edges of the granal thylakoid disks and

pos: MT-ATP8 delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the delta subunit of the catalytic core. Alternatively spliced transcript variants encoding the same isoform have been identified. The MT-ATP8 "gene" encodes a subunit of mitochondrial ATP synthase, located within the thylakoid membrane and the inner mitochondrial membrane. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. The F region causes rotation of F, which has

neg: ATP synthase gamma subunit ATP synthase gamma subunit Gamma subunit of ATP synthase F1 complex forms the central shaft that connects the Fo rotary motor to the F1 catalytic core. F-ATP synthases (also known as F1Fo ATPase, or H(+)-transporting two-sector ATPase) () are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits (alpha, beta, gamma, delta, epsilon), while the Fo ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C), nine in mitochondria (A-G, F6, F8). The human ATP synthase gamma subunit is encoded by the gene ATP5C1.

neg: ATP5F1A ATP5F1A ATP synthase F1 subunit alpha, mitochondrial is an enzyme that in humans is encoded by the "ATP5F1A" gene. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, using an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F, and the membrane-spanning component, F, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single

neg: ATP5B ATP5B ATP synthase F1 subunit beta, mitochondrial is an enzyme that in humans is encoded by the "ATP5F1B" gene. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single

neg: ATP5E ATP5E ATP synthase F1 subunit epsilon, mitochondrial is an enzyme that in humans is encoded by the "ATP5F1E" gene. The protein encoded by ATP5F1E is a subunit of ATP synthase, also known as Complex V. Variations of this gene have been associated with mitochondrial complex V deficiency, nuclear 3 (MC5DN3) and Papillary Thyroid Cancer. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F, and the membrane-spanning component,

neg: ATP5G1 ATP5G1 The "ATP5MC1" gene is one of three human paralogs that encode membrane subunit c of the mitochondrial ATP synthase. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a

neg: ATP synthase alpha/beta subunits make direct contact with the ADP/ATP molecule. ATP5A1; ATP5B; ATP6V1A; ATP6V1B1; ATP6V1B2; ATP synthase alpha/beta subunits ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse, using the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases, which can differ in function (ATP synthesis and/or hydrolysis),

neg: ATP synthase chain as a source of energy. The overall process of creating energy in this fashion is termed oxidative phosphorylation. The same process takes place in the mitochondria, where ATP synthase is located in the inner mitochondrial membrane and the F-part projects into mitochondrial matrix. The consumption of ATP by ATP-synthase pumps proton cations into the matrix. The evolution of ATP synthase is thought to have been modular whereby two functionally independent subunits became associated and gained new functionality. This association appears to have occurred early in evolutionary history, because essentially the same structure and activity of ATP synthase enzymes are

neg: ATP synthase alpha/beta subunits ATP synthase alpha/beta subunits ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse, using the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases, which can differ in function (ATP synthesis and/or hydrolysis), structure (F-, V- and A-ATPases contain rotary motors) and in the type

neg: ATP synthase subunit C ATP synthase subunit C ATPase, subunit C of Fo/Vo complex is the main transmembrane subunit of V-type, A-type and F-type ATP synthases. ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or hydrolysis with the transport of protons across a membrane. ATPases can harness the energy from a proton gradient, using the flux of ions across the membrane via the ATPase proton channel to drive the synthesis of ATP. Some ATPases work in reverse, using the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases, which can differ

neg: Nanoscopic scale cells towards the nucleus and produces the axonemal beating of motile cilia and flagella. "[I]n effect, the [motile cilium] is a nanomachine composed of perhaps over 600 proteins in molecular complexes, many of which also function independently as nanomachines...Flexible linkers allow the mobile protein domains connected by them to recruit their binding partners and induce long-range allostery via . " Other biological machines are responsible for energy production, for example ATP synthase which harnesses energy from proton gradients across membranes to drive a turbine-like motion used to synthesise ATP, the energy currency of a cell. Still other machines are responsible

neg: ATP5B representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the beta subunit of the catalytic core. ATP5B ATP synthase F1 subunit beta, mitochondrial is an enzyme that in humans is encoded by the "ATP5F1B" gene. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of

neg: ATP5F1A none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice and decreased body weight, lean body mass and hypoproteinemia was observed in female animals. ATP5F1A ATP synthase F1 subunit alpha, mitochondrial is an enzyme that in humans is encoded by the "ATP5F1A" gene. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, using an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F, and the membrane-spanning component, F, comprising the proton channel. The

neg: ATP synthase gamma subunit the central shaft that connects the Fo rotary motor to the F1 catalytic core. The gamma subunit functions as a rotary motor inside the cylinder formed by the alpha(3)beta(3) subunits in the F1 complex.</ref> The best-conserved region of the gamma subunit is its C-terminus, which seems to be essential for assembly and catalysis. ATP synthase gamma subunit Gamma subunit of ATP synthase F1 complex forms the central shaft that connects the Fo rotary motor to the F1 catalytic core. F-ATP synthases (also known as F1Fo ATPase, or H(+)-transporting two-sector ATPase) () are composed of two linked complexes: the F1 ATPase

neg: ATP synthase subunit C V-ATPases, there are three proteolipid subunits (c, c′ and c′′) that form part of the proton-conducting pore, each containing a buried glutamic acid residue that is essential for proton transport, and together they form a hexameric ring spanning the membrane. In a recent study c-subunit has been indicated as a critical component of the mitochondrial permeability transition pore. ATP5G1; ATP5G2; ATP5G3; ATP6V0B; ATP6V0C; Diarylquinoline ATP synthase subunit C ATPase, subunit C of Fo/Vo complex is the main transmembrane subunit of V-type, A-type and F-type ATP synthases. ATPases (or ATP synthases) are membrane-bound enzyme complexes/ion transporters that combine ATP synthesis and/or

neg: ATP synthase present in all kingdoms of life. The F-ATP synthase displays high functional and mechanistic similarity to the V-ATPase. However, whereas the F-ATP synthase generates ATP by utilising a proton gradient, the V-ATPase generates a proton gradient at the expense of ATP, generating pH values of as low as 1. The F region also shows significant similarity to hexameric DNA helicases, and the F region shows some similarity to -powered flagellar motor complexes. The αβ hexamer of the F region shows significant structural similarity to hexameric DNA helicases; both form a ring with 3-fold rotational symmetry with a central pore. Both

neg: ATP5J2 (a, b, c, d, e, f, g, F6 and 8). This gene encodes the f subunit of the Fo complex. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. ATP5J2 The "ATP5MF" gene encodes the ATP synthase subunit f, mitochondrial enzyme in humans. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, which comprises the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different

neg: ATP5J2 ATP5J2 The "ATP5MF" gene encodes the ATP synthase subunit f, mitochondrial enzyme in humans. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, which comprises the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and single representatives of the gamma, delta, and epsilon subunits. The proton channel likely has nine subunits

neg: Flutamide of action of flutamide-induced hepatotoxicity is thought to be due to mitochondrial toxicity. Specifically, flutamide and particularly its major metabolite hydroxyflutamide inhibit enzymes in the mitochondrial electron transport chain in hepatocytes, including respiratory complexes I (), II (succinate dehydrogenase), and V (ATP synthase), and thereby reduce cellular respiration via ATP depletion and hence decrease cell survival. Inhibition of taurocholate (a bile acid) efflux has also been implicated in flutamide-induced hepatotoxicity. In contrast to flutamide and hydroxyflutamide, which severely compromise hepatocyte cellular respiration "in vitro", bicalutamide does not significantly do so at the same concentrations and is regarded as non-mitotoxic. It

neg: ATP5J conferral protein), F6, B and D. There is no homologue of subunit F6 in bacterial or chloroplast F-ATPase, whose peripheral stalks are composed of one copy of the delta subunit (homologous to OSCP), and two copies of subunit B in bacteria, or one copy each of subunits B and B' in chloroplasts and photosynthetic bacteria. ATP5J ATP synthase-coupling factor 6, mitochondrial is an enzyme that in humans is encoded by the "ATP5PF" gene. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes:

neg: ATP5E ATP by a long series of experiments in many laboratories. Mitochondrial membrane ATP synthase (FF ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F - containing the extramembraneous catalytic core, and F - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F is coupled via a rotary mechanism of the central stalk subunits to proton

neg: Mitochondrial matrix that contains the complexes of oxidative phosphorylation. which contains the electron transport chain that is found on the cristae of the inner membrane and consists of four protein complexes and ATP synthase. These complexes are Protein complex I (NADH:Coenzyme Q Oxidoreductase), protein complex II (Succinate:Coenzyme Q Oxidoreductase), protein complex III (Coenzyme Q: Cytochrome C Oxidoreductase), and protein complex IV (Cytochrome C Oxidase). The electron transport chain is responsible for establishing a pH and electrochemical gradient that facilitates the production of ATP through the pumping of protons. The gradient also provides control of the concentration of ions such as Ca driven

neg: ATP synthase more ADP and phosphate, ready for the next cycle of ATP production. Like other enzymes, the activity of FF ATP synthase is reversible. Large-enough quantities of ATP cause it to create a transmembrane proton gradient, this is used by fermenting bacteria that do not have an electron transport chain, but rather hydrolyze ATP to make a proton gradient, which they use to drive flagella and the transport of nutrients into the cell. In respiring bacteria under physiological conditions, ATP synthase, in general, runs in the opposite direction, creating ATP while using the proton motive force created by the electron transport

neg: Dynamin-like 120 kDa protein by the oligomerization of two L-OPA1 and one S-OPA1, which then interact with other protein complexes to alter cristae structure. Its cristae regulating function also contributes to its role in oxidative phosphorylation and apoptosis, as it is required to maintain mitochondrial activity during low-energy substrate availability. Moreover, stabilization of mitochondrial cristae by OPA1 protects against mitochondrial dysfunction, cytochrome c release, and reactive oxygen species production, thus preventing cell death. Mitochondrial SLC25A transporters can detect these low levels and stimulate OPA1 oligomerization, leading to tightening of the cristae, enhanced assembly of ATP synthase, and increased ATP production. Stress from an apoptotic

neg: ATP5F1A of experiments in many laboratories. Mitochondrial membrane ATP synthase (FF ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F - containing the extramembraneous catalytic core, and F - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta

neg: Electron transport chain proton gradient). ATP synthase is also readily reversible. Thus ATP can be used to build a proton gradient, which in turn can be used to make NADH. This process of "reverse electron transport" is important in many prokaryotic electron transport chains. In eukaryotes, NADH is the most important electron donor. The associated electron transport chain is NADH → "Complex I" → Q → "Complex III" → cytochrome "c" → "Complex IV" → O where "Complexes I, III" and" IV" are proton pumps, while Q and cytochrome "c" are mobile electron carriers. The electron acceptor is molecular oxygen. In prokaryotes (bacteria

neg: MT-ATP6 the cell nuclear DNA. MT-ATP6 MT-ATP6 (or ATP6) is a mitochondrial gene with the full name 'mitochondrially encoded ATP synthase membrane subunit 6' that encodes the ATP synthase F subunit 6 (or subunit/chain A). This subunit belongs to the F complex of the large, transmembrane F-type ATP synthase. This enzyme, which is also known as complex V, is responsible for the final step of oxidative phosphorylation in the electron transport chain. Specifically, one segment of ATP synthase allows positively charged ions, called protons, to flow across a specialized membrane inside mitochondria. Another segment of the enzyme uses the energy created

neg: Fibril to the shape of the plant via controlled-cell expansion. The stereoscopic arrangement of microfibrils in the cell wall create systems of turgor pressure which ultimately leads to cellular growth and expansion. Cellulose microfibrils are unique matrix macromolecules, in that they are assembled by cellulose synthase enzymes located on the extracellular surface of the plasma membrane. It is believed that the plant can “anticipate their future morphology by controlling the orientation of microfibrils” by a mechanism where cellulose microfibrils are arranged atop a cortical array of microtubules. Stirring of a given sample of amylose is said to form fibrillar crystals which

neg: CTP synthetase two major domains, responsible for the aminotransferase and synthase activity, respectively. The amidotransferase domains are located away from the tetramer interfaces and are not affected by the oligomeric state. The ATP-binding site and CTP-binding site in the synthase domain are located at the tetramer interface. It is for this reason that ATP and UTP are required for tetramerization. CTP synthase is precisely regulated by the intracellular concentrations of CTP and UTP, and both hCTPS1 and hCTPS2 have been seen to be maximally active at physiological concentrations of ATP, GTP, and glutamine. The activity of human CTPS1 isozyme has been demonstrated

neg: ATP5D protein has been known to resemble a 'lollipop' structure due to the attachment of the F1 catalytic unit to the mitochondrial inner membrane by the F0 unit. This gene encodes a subunit of the mitochondrial ATP synthase (Complex V) of the mitochondrial respiratory chain, which is necessary for the catalysis of ATP synthesis. Utilizing an electrochemical gradient of protons produced by electron transport complexes of the respiratory chain, the synthase converts ADP into ATP across the inner membrane during oxidative phosphorylation. F-type ATPases consist of two structural domains, F1 and F0, that contribute to the catalysis. The F1 domain contains

neg: ATP synthase alpha/beta subunits of ions they transport. The alpha and beta (or A and B) subunits are found in the F1, V1, and A1 complexes of F-, V- and A-ATPases, respectively, as well as flagellar ATPase and the termination factor Rho. The F-ATPases (or F1Fo ATPases), V-ATPases (or V1Vo ATPases) and A-ATPases (or A1Ao ATPases) are composed of two linked complexes: the F1, V1 or A1 complex contains the catalytic core that synthesizes/hydrolyses ATP, and the Fo, Vo or Ao complex that forms the membrane-spanning pore. The F-, V- and A-ATPases all contain rotary motors, one that drives proton translocation across the membrane

neg: ATP5J ATP5J ATP synthase-coupling factor 6, mitochondrial is an enzyme that in humans is encoded by the "ATP5PF" gene. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The Fo seems to have nine subunits (a, b,

neg: ATP synthase gamma subunit Both the F1 and Fo complexes are rotary motors that are coupled back-to-back. In the F1 complex, the central gamma subunit forms the rotor inside the cylinder made of the alpha(3)beta(3) subunits, while in the Fo complex, the ring-shaped C subunits forms the rotor. The two rotors rotate in opposite directions, but the Fo rotor is usually stronger, using the force from the proton gradient to push the F1 rotor in reverse in order to drive ATP synthesis. These ATPases can also work in reverse to hydrolyse ATP to create a proton gradient. The ATPase F1 complex gamma subunit forms

neg: ATP5D ATP5D ATP synthase subunit delta, mitochondrial, also known as ATP synthase F1 subunit delta or F-ATPase delta subunit is an enzyme that in humans is encoded by the "ATP5F1D" (formerly "ATP5D") gene. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. The "ATP5F1D" gene is located on the p arm of chromosome 19 at position 13.3 and it spans 3,075 base pairs. The "ATP5F1D" gene produces a 17.5 kDa protein composed of 168 amino acids. The coded protein is a subunit

neg: ATP synthase protons movement across the membrane. The F portion of ATP synthase is hydrophilic and responsible for hydrolyzing ATP. This portion is located through the intermembrane space between the inter membrane space of the mitochondria. Subunits formula_2 and formula_3 make a hexamer with 6 binding sites. Three of them are catalytically inactive and they bind ADP. Other three subunits catalyze the ATP synthesis. The other F subunits formula_4 are a part of a rotational motor mechanism. formula_5 subunit allows formula_3 to go through conformational changes, i.e. closed, half open and open states allows for ATP to be bound and released once

neg: ATP5D of the mitochondrial ATP synthase (Complex V), which is composed of two linked multi-subunit complexes: the soluble catalytic core, F, and the membrane-spanning component, F, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the delta subunit of the catalytic core. Alternatively spliced transcript variants encoding the same isoform have been identified. The structure of the

neg: V-ATPase V-ATPase Vacuolar-type -ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V-ATPases acidify a wide array of intracellular organelles and pump protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that uses the energy from ATP hydrolysis to produce a

neg: ATP synthase subunit C in function (ATP synthesis and/or hydrolysis), structure (F-, V- and A-ATPases contain rotary motors) and in the type of ions they transport. The F-ATPases (or F1Fo ATPases) and V-ATPases (or V1Vo ATPases) are each composed of two linked complexes: the F1 or V1 complex contains the catalytic core that synthesizes/hydrolyses ATP, and the Fo or Vo complex that forms the membrane-spanning pore. The F- and V-ATPases all contain rotary motors, one that drives proton translocation across the membrane and one that drives ATP synthesis/hydrolysis. Subunit C (also called subunit 9, or proteolipid in F-ATPases, or the 16 kDa proteolipid in

neg: Hydrogenosome of a plant or animal is organised very differently from a bacterial cell. Amongst other things, animal and plant cells (which are special cases of what is known as ‘eukaryotic’ cells) contain mitochondria. Mitochondria are like power stations for cells: They supply ATP molecules used throughout the cell as a power source by ‘burning’ carbohydrates and other fuels. They produce carbon dioxide and water as waste. To produce ATP, mitochondria require abundant supplies of oxygen. Some single-celled eukaryotes live in places where oxygen is scarce or non-existent and use hydrogenosomes instead of mitochondria to produce ATP. Mitochondria do not function

neg: Thylakoid the lumen and stroma is high enough to drive ATP synthesis using the ATP synthase. As the protons travel back down the gradient through channels in ATP synthase, ADP + P are combined into ATP. In this manner, the light-dependent reactions are coupled to the synthesis of ATP via the proton gradient. Cyanobacteria are photosynthetic prokaryotes with highly differentiated membrane systems. Cyanobacteria have an internal system of thylakoid membranes where the fully functional electron transfer chains of photosynthesis and respiration reside. The presence of different membrane systems lends these cells a unique complexity among bacteria. Cyanobacteria must be able to

neg: Oxidative phosphorylation cell membrane, rather than the movement of protons. Archaea such as "Methanococcus" also contain the AA synthase, a form of the enzyme that contains additional proteins with little similarity in sequence to other bacterial and eukaryotic ATP synthase subunits. It is possible that, in some species, the AA form of the enzyme is a specialized sodium-driven ATP synthase, but this might not be true in all cases. Molecular oxygen is an ideal terminal electron acceptor because it is a strong oxidizing agent. The reduction of oxygen does involve potentially harmful intermediates. Although the transfer of four electrons and four protons

neg: Phosphorylation the liver (ATP-D-glucose 6-phosphotransferase) and non-specific hexokinase (ATP-D-hexose 6-phosphotransferase). The role of glucose 6-phosphate in glycogen synthase: High blood glucose concentration causes an increase in intracellular levels of glucose 6 phosphate in liver, skeletal muscle and fat (adipose) tissue. (ATP-D-glucose 6-phosphotransferase) and non-specific hexokinase (ATP-D-hexose 6-phosphotransferase). In liver, synthesis of glycogen is directly correlated by blood glucose concentration and in skeletal muscle and adipocytes, glucose has a minor effect on glycogen synthase. High blood glucose releases insulin, stimulating the trans location of specific glucose transporters to the cell membrane. The liver’s crucial role in controlling blood sugar concentrations by breaking

neg: Bedaquiline experienced Since bedaquiline can also prolong the QT interval, use of other QT prolonging drugs should be avoided. Other medications for tuberculosis that can prolong the QT interval include fluoroquinolones and clofazimine. Bedaquiline blocks the proton pump for ATP synthase of mycobacteria. ATP production is required for cellular energy production and its loss leads to cell death, even in dormant or nonreplicating mycobacteria. It is the first member of a new class of drugs called the diarylquinolines. Bedaquiline is bactericidal. The specific part of ATP synthase affected by bedaquiline is subunit c which is encoded by the gene atpE. Mutations

neg: Trypanothione synthase some parasites have in order to obtain drug resistance . Trypanothione synthase In enzymology, a trypanothione synthase () is an enzyme that catalyzes the chemical reaction The 3 substrates of this enzyme are glutathione, glutathionylspermidine, and ATP, whereas its 3 products are N1,N8-bis(glutathionyl)spermidine, ADP, and phosphate. This reaction is especially important for protozoa in the order kinetoplastida as the molecule of N1,N8-bis(glutathionyl)spermidine, also known as trypanothione, is homologous to the function of glutathione in most other prokaryotic and eukaryotic cells. This means that it is a key intermediate in maintaining thiol redox within the cell and defending against harmful oxidative

neg: Trypanothione synthase Trypanothione synthase In enzymology, a trypanothione synthase () is an enzyme that catalyzes the chemical reaction The 3 substrates of this enzyme are glutathione, glutathionylspermidine, and ATP, whereas its 3 products are N1,N8-bis(glutathionyl)spermidine, ADP, and phosphate. This reaction is especially important for protozoa in the order kinetoplastida as the molecule of N1,N8-bis(glutathionyl)spermidine, also known as trypanothione, is homologous to the function of glutathione in most other prokaryotic and eukaryotic cells. This means that it is a key intermediate in maintaining thiol redox within the cell and defending against harmful oxidative effects in such protozoa. This enzyme belongs to the family

neg: Mitochondrial permeability transition pore production. In cell damage resulting from conditions such as neurodegenerative diseases and head injury, opening of the mitochondrial permeability transition pore can greatly reduce ATP production, and can cause ATP synthase to begin hydrolysing, rather than producing, ATP. This produces an energy deficit in the cell, just when it most needs ATP to fuel activity of ion pumps such as the Na/Ca exchanger, which must be activated more than under normal conditions in order to rid the cell of excess calcium. MPT also allows Ca to leave the mitochondrion, which can place further stress on nearby mitochondria, and which can

neg: Energy charge the adenylate energy charge by decreasing the total {ATP+ADP+AMP} concentration. Energy charge The adenylate energy charge is an index used to measure the energy status of biological cells. ATP or Mg-ATP is the principal molecule for storing and transferring energy in the cell : it is used for biosynthetic pathways, maintenance of transmembrane gradients, movement, cell division, etc... More than 90% of the ATP is produced by phosphorylation of ADP by the ATP synthase. ATP can also be produced by “substrate level phosphorylation” reactions (ADP phosphorylation by (1,3)-bisphosphoglycerate, phosphoenolpyruvate, phosphocreatine), by the succinate-CoA ligase and phosphoenolpyruvate carboxylkinase, and by adenylate

neg: Antimycin A subsequently inhibited, as protons are unable to flow through the ATP synthase complex in the absence of a proton gradient. This inhibition also results in the formation of the toxic free radical superoxide. The rate of superoxide production exceeds the cellular mechanisms to scavenge it, overwhelming the cell and leading to cell death. It has also been found to inhibit the cyclic electron flow within photosynthetic systems along the proposed ferredoxin quinone reductase pathway. Although cyanide acts to block the electron transport chain, Antimycin A and cyanide act in different mechanisms. Cyanide binds a site in neighboring protein where iron

neg: Cetrimonium bromide At low concentrations, there are not enough cavities to cause death to the cells, but with increasing the CTAB concentration, more phospholipids are displaced causing more cavities in the membrane leading to cell death. The second proposed method is based on the dissociation of CTAB into CTA and Br within the mitochondrial membrane. The positively charged CTA binds to the ATP synthase not allowing H to bind stopping the synthesis of ATP and resulting in cell death. Cetrimonium bromide Cetrimonium bromide [(CH)N(CH)]Br; cetyltrimethylammonium bromide; hexadecyltrimethylammonium bromide; CTAB] is a quaternary ammonium surfactant. It is one of the components of the

neg: Cellulose synthase (UDP-forming) directions, thus losing its shape viability Plant cellulose synthases belong to the family of glycosyltransferases, which are proteins involved in the biosynthesis and hydrolysis of the bulk of earth's biomass. Cellulose is synthesized by large cellulose synthase complexes (CSCs), which consist of synthase protein isoforms (CesA) that are arranged into a unique hexagonal structure known as a “particle rosette” 50 nm wide and 30–35 nm tall. There are more than 20 of these full-length integral membrane proteins, each of which is around 1000 amino acids long. These rosettes, formerly known as granules, were first discovered in 1972 by electron microscopy

neg: Energy charge Energy charge The adenylate energy charge is an index used to measure the energy status of biological cells. ATP or Mg-ATP is the principal molecule for storing and transferring energy in the cell : it is used for biosynthetic pathways, maintenance of transmembrane gradients, movement, cell division, etc... More than 90% of the ATP is produced by phosphorylation of ADP by the ATP synthase. ATP can also be produced by “substrate level phosphorylation” reactions (ADP phosphorylation by (1,3)-bisphosphoglycerate, phosphoenolpyruvate, phosphocreatine), by the succinate-CoA ligase and phosphoenolpyruvate carboxylkinase, and by adenylate kinase, an enzyme that maintains the three adenine nucleotides in

neg: Microfibril volume increases and the existing microfibrils separate and new ones are formed to help increase cell strength. Cellulose is synthesized by cellulose synthase or Rosette terminal complexes which reside on a cells membrane. As cellulose fibrils are synthesized and grow extracellularly they push up against neighboring cells. Since the neighboring cell can not move easily the Rosette complex is instead pushed around the cell through the fluid phospholipid membrane. Eventually this results in the cell becoming wrapped in a microfibril layer. This layer becomes the cell wall. The organization of microfibrils forming the primary cell wall is rather disorganized. However,

neg: ATP synthase DNA helicase/ motor complex may have had pump activity with the ATPase activity of the helicase driving the motor in reverse. This may have evolved to carry out the reverse reaction and act as an ATP synthase. "E. coli" ATP synthase is the simplest known form of ATP synthase, with 8 different subunit types. Yeast ATP synthase is one of the best-studied eukaryotic ATP synthases; and five F, eight F subunits, and seven associated proteins have been identified. Most of these proteins have homologues in other eukaryotes. In plants, ATP synthase is also present in chloroplasts (CFF-ATP synthase). The enzyme

neg: ATP citrate synthase ATP citrate (pro-S)-lyase. This enzyme participates in citrate cycle (tca cycle) and reductive carboxylate cycle (co2 fixation). ATP citrate synthase In enzymology, an ATP citrate synthase () is an enzyme that catalyzes the chemical reaction The 4 substrates of this enzyme are ADP, phosphate, acetyl-CoA, and oxaloacetate, whereas its 3 products are ATP, citrate, and CoA. This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl-CoA:oxaloacetate C-acetyltransferase [(pro-S)-carboxymethyl-forming, ADP-phosphorylating]. Other names in common use include ATP-citric lyase, ATP:citrate oxaloacetate-lyase [(pro-S)-CH2COO-->acetyl-CoA], (ATP-dephosphorylating),

neg: ATP citrate synthase ATP citrate synthase In enzymology, an ATP citrate synthase () is an enzyme that catalyzes the chemical reaction The 4 substrates of this enzyme are ADP, phosphate, acetyl-CoA, and oxaloacetate, whereas its 3 products are ATP, citrate, and CoA. This enzyme belongs to the family of transferases, specifically those acyltransferases that convert acyl groups into alkyl groups on transfer. The systematic name of this enzyme class is acetyl-CoA:oxaloacetate C-acetyltransferase [(pro-S)-carboxymethyl-forming, ADP-phosphorylating]. Other names in common use include ATP-citric lyase, ATP:citrate oxaloacetate-lyase [(pro-S)-CH2COO-->acetyl-CoA], (ATP-dephosphorylating), acetyl-CoA:oxaloacetate acetyltransferase (isomerizing, ADP-phosphorylating), adenosine triphosphate citrate lyase, citrate cleavage enzyme, citrate-ATP lyase, citric cleavage enzyme, and

neg: Ion transporter These proteins transport ions from high to low concentration with the gradient but in the process ATP is formed. Potential energy in the form of the concentration gradient is used to generate ATP. In animals, this ATP synthesis takes place in the mitochondria using F- type ATPase otherwise known as ATP synthase. V-type ATPase serves the opposite function as F-type ATPase and is used in plants to hydrolyze ATP to create a proton gradient. Examples of this are lysosomes that use V-type ATPase acidify vesicles or plant vacuoles during process of photosynthesis in the chloroplasts. This process can be regulated

neg: ATP synthase ATP synthase ATP synthase is an enzyme that creates the energy storage molecule adenosine triphosphate (ATP). ATP is the most commonly used "energy currency" of cells for all organisms. It is formed from adenosine diphosphate (ADP) and inorganic phosphate (P). The overall reaction catalyzed by ATP synthase is: The formation of ATP from ADP and P is energetically unfavorable and would normally proceed in the reverse direction. In order to drive this reaction forward, ATP synthase couples ATP synthesis during cellular respiration to an electrochemical gradient created by the difference in proton (H) concentration across the mitochondrial membrane in eukaryotes

neg: Adenine nucleotide translocator adenine nucleotides takes place by the ANT. The ANT and the F0-F1 ATP synthase are not necessarily in directional synchrony. Apart from exchange of ADP and ATP across the inner mitochondrial membrane, the ANT also exhibits an intrinsic uncoupling activity ANT is an important modulatory but not structural component of the mitochondrial permeability transition pore which can open and lead to cell death through apoptosis or necrosis. In humans, there exist three paraologous ANT isoforms: Adenine nucleotide translocator Adenine nucleotide translocator (ANT), also known as the ADP/ATP translocase, exchanges free ATP with free ADP across the inner mitochondrial membrane. ANT

neg: ATPC RNA motif ATPC RNA motif The ATPC RNA motif is a conserved RNA structure found in certain cyanobacteria. It is apparently ubiquitous in "Prochlorococcus marinus", and is present in many species in the genus "Synechococcus". The RNA is always found within an operon encoding subunits of ATP synthase, and it is always located downstream of the gene encoding the A subunit of ATP synthase, and upstream of the C subunit gene. This location is consistent with a cis-regulatory element, but also with a non-coding RNA that is transcribed with the ATP synthase genes. Simple RNA structures called stem-loops have been reported in

neg: ATPC RNA motif the ATP synthase operons of various cyanobacteria, but not structures such as the 3-stem junction that is the main feature of the ATPC RNA motif. ATPC RNA motif The ATPC RNA motif is a conserved RNA structure found in certain cyanobacteria. It is apparently ubiquitous in "Prochlorococcus marinus", and is present in many species in the genus "Synechococcus". The RNA is always found within an operon encoding subunits of ATP synthase, and it is always located downstream of the gene encoding the A subunit of ATP synthase, and upstream of the C subunit gene. This location is consistent with a

neg: USMG5 USMG5 Up-regulated during skeletal muscle growth protein 5 (USMG5), also known as ATP synthase membrane subunit DAPIT (ATP5MD), Diabetes-associated protein in insulin-sensitive tissues, or HCV F-transactivated protein 2 is a protein that in humans is encoded by the "USMG5" gene. The "USMG5" gene is located on the q arm of chromosome 10 at position 24.33 and it spans 7,463 base pairs. The "USMG5" gene produces a 6.46 kDa protein composed of 58 amino acids. USMG5 is a small subunit of the mitochondrial ATP synthase (complex V), as well as the lysosomal V-ATPase. The protein is associated with the ATP synthase

neg: Paraptosis of PEBP and/or other kinase inhibitors seem to indicate participation in the MAPK and JNK pathways, as diminished PEBP would allow for the levels of MAPK and JNK to accumulate enough to be sufficient to induce cell death. ATP synthase is composed of multiple subunits and found in the mitochondria. When undergoing paraptosis, higher amounts of ATP synthase ß-subunit were demonstrated in P20. Mitochondrial staining reveals that rounded paraptotic cells with elevated levels of prohibitin appear to be undergoing reorganization of the mitochondrial network. Paratotic cells demonstrated a 3.4 fold increased in prohibitin. Increased levels of prohibitin in conjugation with

neg: Cellulose synthase (UDP-forming) biosynthesis of primary cell walls throughout the whole plant while the AtCesA7 (IRX3) protein is only expressed in the stem for secondary cell wall production. Cellulose biosynthesis is the process during which separate homogeneous β-(1→4)-glucan chains, ranging from 2,000 to 25,000 glucose residues in length, are synthesized and then immediately hydrogen bond with one another to form rigid crystalline arrays, or microfibrils. Microfibrils in the primary cell wall are approximately 36 chains long while those of the secondary cell wall are much larger, containing up to 1200 β-(1→4)-glucan chains. Uridine diphosphate-glucose (UDP), which is produced by the enzyme sucrose synthase

neg: Dinoseb because of the electrochemical gradient that exists across the IMM. By lowering the proton gradient, dinoseb removes the cell’s ability to produce ATP, resulting in the death of the cell. In plants, dinoseb also inhibits photosynthesis by inhibiting the electron flow from photocomplex II to plastoquinone. As a result, the plastoquinone can’t create a proton gradient and no ATP is produced by the ATP synthase. Also, NADP can’t be reduced to form NADPH, which removes the ability to create glucose from carbon dioxide. This also leads to cell death. After oral administration of dinoseb tagged with C to rats and

neg: Reactive oxygen species enough time for the molecule to travel into the nucleus of the cell, subsequently reacting with macromolecules such as DNA. ROS are produced intracellularly through multiple mechanisms and depending on the cell and tissue types, the major sources being the "professional" producers of ROS: NADPH oxidase (NOX) complexes (7 distinct isoforms) in cell membranes, mitochondria, peroxisomes, and endoplasmic reticulum. Mitochondria convert energy for the cell into a usable form, adenosine triphosphate (ATP). The process in which ATP is produced, called oxidative phosphorylation, involves the transport of protons (hydrogen ions) across the inner mitochondrial membrane by means of the electron transport

neg: Archaea are extremely diverse, and range from the oxidation of ammonia by the Nitrosopumilales to the oxidation of hydrogen sulfide or elemental sulfur by species of "Sulfolobus", using either oxygen or metal ions as electron acceptors. Phototrophic archaea use light to produce chemical energy in the form of ATP. In the Halobacteria, light-activated ion pumps like bacteriorhodopsin and halorhodopsin generate ion gradients by pumping ions out of and into the cell across the plasma membrane. The energy stored in these electrochemical gradients is then converted into ATP by ATP synthase. This process is a form of photophosphorylation. The ability of these

neg: Thymosin beta-4 surface-located ATP synthase, which would allow extracellular thymosin to signal via a purinergic receptor. Some of the multiple activities of thymosin β unrelated to actin may be mediated by a tetrapeptide enzymically-cleaved from its N-terminus, N-acetyl-ser-asp-lys-pro, brand names Seraspenide or Goralatide, best known as an inhibitor of the proliferation of haematopoietic (blood-cell precursor) stem cells of bone marrow. Work with cell cultures and experiments with animals have shown that administration of thymosin β can promote migration of cells, formation of blood vessels, maturation of stem cells, survival of various cell types and lowering of the production of pro-inflammatory cytokines. These

neg: ATP synthase the enzyme because of the high concentration of mitochondria in cardiac muscle. The following is a list of humans genes that encode components of ATP synthases: ATP synthase ATP synthase is an enzyme that creates the energy storage molecule adenosine triphosphate (ATP). ATP is the most commonly used "energy currency" of cells for all organisms. It is formed from adenosine diphosphate (ADP) and inorganic phosphate (P). The overall reaction catalyzed by ATP synthase is: The formation of ATP from ADP and P is energetically unfavorable and would normally proceed in the reverse direction. In order to drive this reaction forward,

neg: Active transport instead it relies upon the electrochemical potential difference created by pumping ions in/out of the cell. Permitting one ion or molecule to move down an electrochemical gradient, but possibly against the concentration gradient where it is more concentrated to that where it is less concentrated increases entropy and can serve as a source of energy for metabolism (e.g. in ATP synthase). The energy derived from the pumping of protons across a cell membrane is frequently used as the energy source in secondary active transport. In humans, sodium (Na) is a commonly co-transported ion across the plasma membrane, whose electrochemical gradient

neg: Eyespot (wheat) cell wall. A specific sequence of enzymes is employed; without these enzymes the fungus would not be able to invade the plant cell. The process begins with breaking of the leaf cuticle by formation of appressoria which provide the mechanical force to break into the cell. Then Pectin, cellulase, hemicellulase and protease enzymes are released to enable invasion into the host cell. Now the fungus is present in the plant stem, it causes disease by affecting nutrient and water supply to upper parts of the plant, weakening the plant stem. In some cases beta, 1-3 glycan synthase is also released

neg: Citrate synthase family MgATP-dependent, CoA-dependent cleavage of citrate into oxaloacetate and acetyl-CoA, a key step in the reductive tricarboxylic acid pathway of CO assimilation used by a variety of autotrophic bacteria and archaea to fix carbon dioxide. ATP citrate synthase is composed of two distinct subunits. In eukaryotes, ATP citrate synthase is a homotetramer of a single large polypeptide, and is used to produce cytosolic acetyl-CoA from mitochondrial produced citrate. Citrate synthase family In molecular biology, the citrate synthase family of proteins includes the enzymes citrate synthase , and the related enzymes 2-methylcitrate synthase and ATP citrate synthase . Citrate synthase is a

neg: Electron transport chain by Nobel Prize in Chemistry winner Peter D. Mitchell, the electron transport chain and oxidative phosphorylation are coupled by a proton gradient across the inner mitochondrial membrane. The efflux of protons from the mitochondrial matrix creates an electrochemical gradient (proton gradient). This gradient is used by the FF ATP synthase complex to make ATP via oxidative phosphorylation. ATP synthase is sometimes described as "Complex V" of the electron transport chain. The F component of ATP synthase acts as an ion channel that provides for a proton flux back into the mitochondrial matrix. It is composed of a, b and c

neg: MT-ATP8 MT-ATP8 MT-ATP8 (or ATP8) is a mitochondrial gene with the full name 'mitochondrially encoded ATP synthase membrane subunit 8' that encodes a subunit of mitochondrial ATP synthase, ATP synthase F subunit 8 (or subunit A6L). This subunit belongs to the F complex of the large, transmembrane F-type ATP synthase. This enzyme, which is also known as complex V, is responsible for the final step of oxidative phosphorylation in the electron transport chain. Specifically, one segment of ATP synthase allows positively charged ions, called protons, to flow across a specialized membrane inside mitochondria. Another segment of the enzyme uses the energy

neg: ATP synthase nucleotide binding sites to go through a series of conformational changes that lead to ATP synthesis. The major F subunits are prevented from rotating in sympathy with the central stalk rotor by a peripheral stalk that joins the alphabeta to the non-rotating portion of F. The structure of the intact ATP synthase is currently known at low-resolution from electron cryo-microscopy (cryo-EM) studies of the complex. The cryo-EM model of ATP synthase suggests that the peripheral stalk is a flexible structure that wraps around the complex as it joins F to F. Under the right conditions, the enzyme reaction can also

neg: CTP synthetase synthase remains a model enzyme for the study of filament formation. Upregulated CTP synthase activity has been widely seen in human and rodent tumors. Mutations in the CTP synthase have been seen to confer resistance to cytotoxic drugs such as cytosine arabinoside (ara-C) in a Chinese hamster ovary (CHO) cell model of leukemia though such mutations were not found in human patients with ara-C resistance. CTP synthetase CTP synthetase is an enzyme involved in pyrimidine biosynthesis that interconverts UTP and CTP. CTP (cytidine triphosphate) synthetase catalyzes the last committed step in pyrimidine nucleotide biosynthesis: ATP + UTP + glutamine →

neg: Diarylquinoline produce heteroaromatic quinoline derivatives. Diarylquinoline Diarylquinolines (DARQs) is a chemical class of drugs that treat tuberculosis, They target subunit c of mycobacterial ATP synthase, inhibiting the enzyme so mycobacterium tuberculosis cannot synthesise ATP. This effectively kills the bacteria. Although ATP synthase in bacteria is similar to its eukaryotic analogue, diarylquinoline agents (such as TMC207) are very specific to the bacterial enzyme, so were expected to be safe for use in humans and other eukaryotes. This also suggests that bacterial ATP synthase inhibition is an attractive therapeutic target The reaction of arylaldehyde, malonodinitrile, and 3‐arylamino‐5,5‐dimethylcyclohex‐2‐enone can produce 1,4-diarylquinolines. The reaction of

neg: Diarylquinoline Diarylquinoline Diarylquinolines (DARQs) is a chemical class of drugs that treat tuberculosis, They target subunit c of mycobacterial ATP synthase, inhibiting the enzyme so mycobacterium tuberculosis cannot synthesise ATP. This effectively kills the bacteria. Although ATP synthase in bacteria is similar to its eukaryotic analogue, diarylquinoline agents (such as TMC207) are very specific to the bacterial enzyme, so were expected to be safe for use in humans and other eukaryotes. This also suggests that bacterial ATP synthase inhibition is an attractive therapeutic target The reaction of arylaldehyde, malonodinitrile, and 3‐arylamino‐5,5‐dimethylcyclohex‐2‐enone can produce 1,4-diarylquinolines. The reaction of enamides and imines can

neg: V-ATPase of alternating A and B subunits, a central rotor D, peripheral stators G and E, and regulatory subunits C and H. Hydrolysis of ATP drives a conformational change in the six A|B interfaces and with it rotation of the central rotor D. Unlike with the ATP synthase, the V domain is not an active ATPase when dissociated. In molecular biology, V-ATPase (Vacuolar-ATPase) C represents the C terminal subunit that is part of the V1 complex, and is localised to the interface between the V1 and V0 complexes. The C subunit plays an essential role in controlling the assembly of V-ATPase,

neg: ATP5E has been shown to have 34 binary protein-protein interactions including 28 co-complex interactions. ATP5F1E appears to interact with ATP5F1D, AGTRAP, CYP17A1, UBE2N. ATP5E ATP synthase F1 subunit epsilon, mitochondrial is an enzyme that in humans is encoded by the "ATP5F1E" gene. The protein encoded by ATP5F1E is a subunit of ATP synthase, also known as Complex V. Variations of this gene have been associated with mitochondrial complex V deficiency, nuclear 3 (MC5DN3) and Papillary Thyroid Cancer. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner

neg: ATP5D associated with the catalytic core. The catalytic core is composed of five different subunits including alpha, beta, gamma, delta, and epsilon subunits. The protein has additional interactions with ATP5I, ATP5O, PUS1, NDUFB5, GTPBP6, ATP5L, ATP5J and others. ATP5D ATP synthase subunit delta, mitochondrial, also known as ATP synthase F1 subunit delta or F-ATPase delta subunit is an enzyme that in humans is encoded by the "ATP5F1D" (formerly "ATP5D") gene. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. The "ATP5F1D" gene

neg: TMEM70 TMEM70 Transmembrane protein 70 is a protein that in humans is encoded by the "TMEM70" gene. It is a transmembrane protein located in the mitochondrial inner membrane involved in the assembly of the F1 and Fo structural subunits of ATP synthase. Mutations in this gene have been associated with neonatal mitochondrial encephalo-cardiomyopathy due to ATP synthase (Complex V) deficiency, causing a wide variety of symptoms including 3-methylglutaconic aciduria, lactic acidosis, mitochondrial myopathy, and cardiomyopathy. The "TMEM70" gene has 4 exons and is located on the q arm of chromosome 8 in position 21.11 and spans 6,642 base pairs. The gene

neg: Proton pump inner membrane where is functions as a proton transport-driven ATP synthase. In mitochondria, reducing equivalents provided by electron transfer or photosynthesis power this translocation of protons. For example, the translocation of protons by cytochrome c oxidase is powered by reducing equivalents provided by reduced cytochrome c. ATP itself powers this transport in the plasma membrane proton ATPase and in the ATPase proton pumps of other cellular membranes. The FF ATP synthase of mitochondria, in contrast, usually conduct protons from high to low concentration across the membrane while drawing energy from this flow to synthesize ATP. Protons translocate across the inner

neg: Xylan backbone . Studies on Arabidopsis mutants revealed that several Glycosyltransferase are involved in the biosynthesis of xylans. Glycosyltransferases (GTs) catalyze the formation of glycosidic bonds between sugar molecules using nucleotide sugar as donor molecule . In eukaryotes, GTs represent about 1% to 2% of gene products . GTs are assembled into complexes existing in the Golgi apparatus. However, no xylan synthase complexes have been isolated from "Arabidopsis" tissues (dicot). The first gene involved in the biosynthesis of xylan was revealed on xylem mutants (irx) in Arabidopsis thaliana because of some mutation affecting xylan biosynthesis genes. As a result, abnormal plant

neg: USMG5 ATP synthase complex, and has co-complex interactions with ATP5F1, ATP5MC1, TP5F1E, ATP5H, ATP5ME, ATP5J, ATP5J2, and others. USMG5 Up-regulated during skeletal muscle growth protein 5 (USMG5), also known as ATP synthase membrane subunit DAPIT (ATP5MD), Diabetes-associated protein in insulin-sensitive tissues, or HCV F-transactivated protein 2 is a protein that in humans is encoded by the "USMG5" gene. The "USMG5" gene is located on the q arm of chromosome 10 at position 24.33 and it spans 7,463 base pairs. The "USMG5" gene produces a 6.46 kDa protein composed of 58 amino acids. USMG5 is a small subunit of the mitochondrial ATP

neg: Carnosine synthase The gene encoding the Carnosine synthase is ATPGD1, a member of the “ATP-grasp family” of ligases. Because of its involvement in the formation of carnosine, this gene is now also named 'CARNS1'. Carnosine synthase Carnosine synthase () is an enzyme that catalyzes the chemical reaction The 3 substrates of this enzyme are ATP, L-histidine, and beta-alanine, whereas its 3 products are ADP (previously thought to form AMP), diphosphate, and carnosine. This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). The systematic name of this enzyme class is 'L-histidine:beta-alanine ligase (AMP-forming)' (incorrect

neg: ATP5F1 subunits b and b' in chloroplasts and photosynthetic bacteria. ATP5F1 ATP synthase subunit b, mitochondrial is an enzyme that in humans is encoded by the "ATP5PB" gene. The b subunits are part of the peripheral stalk that links the F1 and FO complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element. The peripheral stalk differs in subunit composition between mitochondrial, chloroplast and bacterial F-ATPases. In bacterial and chloroplast F-ATPases, the peripheral stalk is composed of one copy of the delta subunit (homologous to OSCP in mitochondria), and two copies of

neg: ATP5F1 ATP5F1 ATP synthase subunit b, mitochondrial is an enzyme that in humans is encoded by the "ATP5PB" gene. The b subunits are part of the peripheral stalk that links the F1 and FO complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element. The peripheral stalk differs in subunit composition between mitochondrial, chloroplast and bacterial F-ATPases. In bacterial and chloroplast F-ATPases, the peripheral stalk is composed of one copy of the delta subunit (homologous to OSCP in mitochondria), and two copies of subunit b in bacteria, or one copy each of

neg: Molecular machine for muscle contraction, kinesin, which moves cargo inside cells away from the nucleus along microtubules, and dynein, which moves cargo inside cells towards the nucleus and produces the axonemal beating of motile cilia and flagella. "[I]n effect, the [motile cilium] is a nanomachine composed of perhaps over 600 proteins in molecular complexes, many of which also function independently as nanomachines...Flexible linkers allow the mobile protein domains connected by them to recruit their binding partners and induce long-range allostery via . " Other biological machines are responsible for energy production, for example ATP synthase which harnesses energy from proton gradients across

neg: Trypanothione synthase the cells which did not contain working trypanothione synthase had a much higher death rate than wild type T. brucei. The current believed mechanism for synthetase activity is that first glutathione and Mg-ATP bind to the enzyme in a ternary complex where glutathione becomes activated by ATP and forms glutathionyl phosphate. ADP then leaves the active site and the activated phosphate still bound to the enzyme in what is equivalent to a substituted enzyme reacts with glutathionylspermidine to form trypanothione. The regulation of trypanothione synthase is currently thought to be driven by conformational changes caused by allosteric interactions as the

neg: AICA ribonucleotide this is protective. Preconditioning preceded myocardial infarction, may delay cell death and allow for greater salvage of myocardium through reperfusion therapy. AICAR has been shown to precondition the heart shortly before or during ischemia. AICAR triggers a preconditioned anti-inflammatory state by increasing NO production from endothelial nitric oxide synthase. When AICAR is given 24 hours prior to reperfusion, it prevents post ischemic leukocyte-endothelial cell adhesive interactions with increased NO production. AICAR-dependent preconditioning is also mediated by an ATP-sensitive potassium channel and hemeoxygenase-dependent mechanism. It increases AMPK-dependent recruitment of ATP-sensitive K channels to the sarcolemma causing the action potential duration to

neg: MT-ATP6 testing of the aforementioned mitochondrial genes, including MT-ATP6. MT-ATP6 gene mutations associated with Leigh syndrome change one DNA building block (nucleotide) in the MT-ATP6 gene. The most common genetic change replaces the nucleotide thymine with guanine at position 8993 (written as T8993G). The mutations that cause Leigh syndrome impair the function or stability of the ATP synthase complex, inhibiting ATP production and impairing oxidative phosphorylation. Although the exact mechanism is unclear, researchers believe that impaired oxidative phosphorylation can lead to cell death because of decreased energy available in the cell. Certain tissues that require large amounts of energy, such as