Dimethylmalate dehydrogenase

dimethylmalate dehydrogenase
Identifiers
EC no.1.1.1.84
CAS no.37250-21-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

In enzymology, dimethylmalate dehydrogenase (EC 1.1.1.84) is an enzyme that catalyzes the chemical reaction

(R)-3,3-dimethylmalic acid
 
 
 
H+
 
H+
 
+ CO2 + NADH
 

The two substrates of this enzyme are (R)-3,3-dimethylmalic acid and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are α-ketoisovaleric acid, carbon dioxide, reduced NADH, and a proton.[1][2]

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

  1. ^ Enzyme 1.1.1.84 at KEGG Pathway Database.
  2. ^ 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.