3-(imidazol-5-yl)lactate dehydrogenase

3-(imidazol-5-yl)lactate dehydrogenase
Identifiers
EC no.1.1.1.111
CAS no.37250-42-3
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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In enzymology, 3-(imidazol-5-yl)lactate dehydrogenase (EC 1.1.1.111) is an enzyme that catalyzes the chemical reaction

(S)-3-(imidazol-5-yl)lactic acid
 
 
 
H+
 
H+
 
imidazole-4-pyruvic acid
 

The two substrates of this enzyme are (S)-3-(imidazol-5-yl)lactic acid and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are imidazole-4-pyruvic acid, reduced NADH, and a proton. The enzyme can use the alternative cofactor, nicotinamide adenine dinucleotide phosphate.[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 (S)-3-(imidazol-5-yl)lactate:NAD(P)+ oxidoreductase. This enzyme is also called imidazol-5-yl lactate dehydrogenase.

References

  1. ^ Enzyme 1.1.1.111 at KEGG Pathway Database.
  2. ^ Coote JG, Hassall H (January 1969). "The role of imidazol-5-yl-lactate-nicotinamide-adenine dinucleotide phosphate oxidoreductase and histidine-2-oxoglutarate aminotransferase in the degradation of imidazol-5-yl-lactate by Pseudomonas acidovorans". The Biochemical Journal. 111 (2): 237–9. doi:10.1042/bj1110237. PMC 1187811. PMID 4303364.
  3. ^ Cortese R, Brevet J, Hedegaard J, Roche J (1968). "[Identification and purification of an alpha-ketoacid aromatic reductase of Escherichia coli B]". Comptes Rendus des Séances de la Société de Biologie et de ses Filiales (in French). 162 (2): 390–5. PMID 4237631.