Malate dehydrogenase (quinone)
| malate dehydrogenase (quinone) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.5.4 | ||||||||
| CAS no. | 71822-24-7 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, malate dehydrogenase (quinone) (EC 1.1.5.4), formerly malate dehydrogenase (acceptor) (EC 1.1.99.16), is an enzyme that catalyzes the chemical reaction
The two substrates of this enzyme are (S)-malic acid and a quinone. Its products are oxaloacetic acid and reduced quinone. The cofactor can be a variety of quinones including vitamin K.[1][2][3]
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with a quinone as acceptor. The systematic name of this enzyme class is (S)-malate:quinone oxidoreductase. Other names in common use include FAD-dependent malate-vitamin K reductase, malate-vitamin K reductase, and (S)-malate:(quinone) oxidoreductase. This enzyme participates in pyruvate metabolism. It employs one cofactor, FAD.
References
[edit]- ↑ Enzyme 1.1.5.4 at KEGG Pathway Database.
- ↑ Imai D; Brodie AF (1973). "A phospholipid-requiring enzyme, malate-vitamin K reductase". J. Biol. Chem. 248 (21): 7487–7494. doi:10.1016/S0021-9258(19)43316-4.
- Imai T (1978). "FAD-dependent malate dehydrogenase, a phospholipid-requiring enzyme from Mycobacterium sp. strain Takeo. Purification and some properties". Biochim. Biophys. Acta. 523 (1): 37–46. doi:10.1016/0005-2744(78)90006-2. PMID 629992.
- ↑ Prasada Reddy TL, Suryanarayana Murthy P, Venkitasubramanian TA (1975). "Variations in the pathways of malate oxidation and phosphorylation in different species of Mycobacteria". Biochim. Biophys. Acta. 376 (2): 210–8. doi:10.1016/0005-2728(75)90012-2. PMID 234747.
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