Dimethylmalate dehydrogenase
Appearance
dimethylmalate dehydrogenase | |||||||||
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Identifiers | |||||||||
EC no. | 1.1.1.84 | ||||||||
CAS no. | 37250-21-8 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a dimethylmalate dehydrogenase (EC 1.1.1.84) is an enzyme that catalyzes the chemical reaction
- (R)-3,3-dimethylmalate + NAD+ 3-methyl-2-oxobutanoate + CO2 + NADH
Thus, the two substrates of this enzyme are (R)-3,3-dimethylmalate and NAD+, whereas its 3 products are 3-methyl-2-oxobutanoate, CO2, and NADH.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-3,3-dimethylmalate:NAD+ oxidoreductase (decarboxylating). This enzyme is also called beta,beta-dimethylmalate dehydrogenase. This enzyme participates in pantothenate and coa biosynthesis. It has 5 cofactors: ammonia, manganese, cobalt, potassium, and NH4+.
References
[edit]- Magee PT, Snell EE (1966). "The bacterial degradation of pantothenic acid. IV. Enzymatic conversion of aldopantoate to alpha-ketoisovalerate". Biochemistry. 5 (2): 409–16. doi:10.1021/bi00866a004. PMID 4287371.