(R,R)-butanediol dehydrogenase

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(R,R)-butanediol dehydrogenase
1geg assembly.png
Meso-2,3-butanediol dehydrogenase from Klebsiella pneumoniae. PDB 1geg
Identifiers
EC no. 1.1.1.4
CAS no. 37250-09-2
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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PMC articles
PubMed articles
NCBI proteins

In enzymology, a (R,R)-butanediol dehydrogenase (EC 1.1.1.4) is an enzyme that catalyzes the chemical reaction

+ NAD+
 
 
 
H+
Biochem reaction arrow reversible NYYN horiz med.svg
 
H+
 
(R)-Acetoin.svg
R-acetoin
+ NADH
 

The two substrates of this enzyme are (R,R)-butane-2,3-diol and NAD+; its products are (R)-acetoin, nicotinamide adenine dinucleotide (NADH), and a proton. [1] [2] [3]

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,R)-butane-2,3-diol:NAD+ oxidoreductase. Other names in common use include butyleneglycol dehydrogenase, D-butanediol dehydrogenase, D-(−)-butanediol dehydrogenase, butylene glycol dehydrogenase, diacetyl (acetoin) reductase, D-aminopropanol dehydrogenase, D-aminopropanol dehydrogenase, 1-amino-2-propanol dehydrogenase, 2,3-butanediol dehydrogenase, D-1-amino-2-propanol dehydrogenase, (R)-diacetyl reductase, (R)-2,3-butanediol dehydrogenase, D-1-amino-2-propanol:NAD+ oxidoreductase, 1-amino-2-propanol oxidoreductase, and aminopropanol oxidoreductase. This enzyme participates in butanoic acid metabolism.

References

  1. Enzyme 1.1.1.4 at KEGG Pathway Database.
  2. Strecker HJ, Harary I (November 1954). "Bacterial butylene glycol dehydrogenase and diacetyl reductase". The Journal of Biological Chemistry. 211 (1): 263–70. doi: 10.1016/S0021-9258(18)71216-7 . PMID   13211662.
  3. Taylor MB, Juni E (April 1960). "Stereoisomeric specificities of 2,3-butanediol dehydrogenases". Biochimica et Biophysica Acta. 39 (3): 448–57. doi:10.1016/0006-3002(60)90197-9. PMID   13837186.