 | This article may require
cleanup to meet Wikipedia's
quality standards. The specific problem is: Need to explain the deletion of EC due to being "covered by
EC 7.1.1.2" (the ubiquinone one). Such a merge makes sense for some proteins tagged with that EC, but definitely does not make sense for this article. (April 2022) |
| NADH dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 7.1.1.2 | ||||||||
| CAS no. | 9079-67-8 | ||||||||
| Alt. names | cytochrome c reductase, type 1 dehydrogenase, beta-NADH dehydrogenase dinucleotide, diaphorase, dihydrocodehydrogenase I dehydrogenase, dihydronicotinamide adenine dinucleotide dehydrogenase, diphosphopyridine diaphorase, DPNH diaphorase, NADH diaphorase, NADH hydrogenase, NADH oxidoreductase, NADH-menadione oxidoreductase, reduced diphosphopyridine nucleotide diaphorase [1] | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
NADH dehydrogenase is an enzyme that converts nicotinamide adenine dinucleotide (NAD) from its reduced form (NADH) to its oxidized form (NAD+). Members of the NADH dehydrogenase family and analogues are commonly systematically named using the format NADH:acceptor oxidoreductase. [2] [3] [4] [5] The chemical reaction these enzymes catalyze is generally represented with the following equation:
- NADH + H+ + acceptor ⇌ NAD+ + reduced acceptor
NADH dehydrogenase is a flavoprotein that contains iron-sulfur centers.
NADH dehydrogenase is used in the electron transport chain for generation of ATP.
The EC term NADH dehydrogenase (quinone) (EC 1.6.5.11) is defined for NADH dehydrogenases that use a quinone (excluding ubiquinone) as the acceptor. The EC term NADH dehydrogenase (ubiquinone) (EC 7.1.1.2) is defined for those with ubiquinone as the acceptor.
References
- ^ EC 1.6.99.3
- ^ Adachi K, Okuyama T (June 1972). "Study on the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes. I. Crystallization and properties of the reduced pyridine nucleotide dehydrogenase of bovine erythrocytes". Biochimica et Biophysica Acta (BBA) - Enzymology. 268 (3): 629–37. doi: 10.1016/0005-2744(72)90266-5. PMID 4402556.
- ^ Hatefi, Y.; Ragan, C.I.; Galante, Y.M. (1985). "The enzymes and the enzyme complexes of the mitochondrial oxidative phosphorylation system". In Martonosi, A. (ed.). The Enzymes of Biological Membranes. Vol. 4 (2nd ed.). New York: Plenum Press. pp. 1–70.
- ^ Hochstein LI, Dalton BP (April 1973). "Studies of a halophilic NADH dehydrogenase. I. Purification and properties of the enzyme". Biochimica et Biophysica Acta (BBA) - Enzymology. 302 (2): 216–28. doi: 10.1016/0005-2744(73)90150-2. PMID 4144655.
- ^ Kaniuga Z (August 1963). "The transformation of mitochondrial NADH dehydrogenase into NADH: Cytochrome c oxidoreductase". Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects. 73 (4): 550–64. doi: 10.1016/0926-6569(63)90175-5. PMID 14074130.
External links
- NADH+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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