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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 (Pi). The overall reaction catalyzed by ATP synthase is:
MT-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 Fo subunit 8. This subunit belongs to the Fo 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 by this proton flow to convert a molecule called adenosine diphosphate (ADP) to ATP. Subunit 8 differs in sequence between Metazoa, plants and Fungi.
ATPase, subunit C of Fo/Vo complex is the main transmembrane subunit of V-type, A-type and F-type ATP synthases.
ATP synthase F1 subunit beta, mitochondrial is an enzyme that in humans is encoded by the ATP5F1B gene.
ATP synthase F1 subunit alpha, mitochondrial is an enzyme that in humans is encoded by the ATP5F1A gene.
ATP synthase-coupling factor 6, mitochondrial is an enzyme that in humans is encoded by the ATP5PF gene.
The ATP5MF gene encodes the ATP synthase subunit f, mitochondrial enzyme in humans.
ATPases 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.
ATP synthase delta subunit is a subunit of bacterial and chloroplast ATPase. It is known as OSCP in mitochondrial ATPase.
ATP synthase subunit g, mitochondrial is an enzyme that in humans is encoded by the ATP5MG gene.
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 are composed of two linked complexes: the F1 ATPase complex is the catalytic core and is composed of 5 subunits, while the Fo ATPase complex is the membrane-embedded proton channel that is composed of at least 3 subunits (A-C), nine in mitochondria.
The human ATP5F1C gene encodes the gamma subunit of an enzyme called mitochondrial ATP synthase.
ATP synthase subunit b, mitochondrial is an enzyme that in humans is encoded by the ATP5PB gene.
ATP synthase subunit s, mitochondrial is an enzyme that in humans is encoded by the ATP5S gene.
The ATP5MC2 gene is one of three human paralogs that encode membrane subunit c of the mitochondrial ATP synthase.
ATP synthase subunit e, mitochondrial is an enzyme that in humans is encoded by the ATP5ME gene.
The human gene ATP5PD encodes subunit d of the peripheral stalk part of the enzyme mitochondrial ATP synthase.
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 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 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.
The ATP5MC3 gene is one of three human paralogs that encode membrane subunit c of the mitochondrial ATP synthase.
References
- ↑ Ahmad Z, Okafor F, Laughlin TF (2011). "Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase". Journal of Amino Acids. 2011: 1–12. doi:10.4061/2011/785741. PMC 3268026 . PMID 22312470.
- ↑ Keis, S; Stocker, A; Dimroth, P; Cook, GM (June 2006). "Inhibition of ATP hydrolysis by thermoalkaliphilic F1Fo-ATP synthase is controlled by the C terminus of the epsilon subunit". Journal of bacteriology. 188 (11): 3796–804. doi:10.1128/JB.00040-06. PMID 16707672.
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