(R)-4-hydroxyphenyllactate dehydrogenase

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(R)-4-hydroxyphenyllactate dehydrogenase
Identifiers
EC no. 1.1.1.222
CAS no. 101754-02-3
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

(R)-4-hydroxyphenyllactate dehydrogenase (EC 1.1.1.222) is an enzyme that catalyzes a chemical reaction

+ NAD+
 
 
 
H+
Biochem reaction arrow reversible NYYN horiz med.svg
 
H+
 
+ NADH
 

The substrates of this enzyme are (R)-3-(4-hydroxyphenyl)lactate and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are 3-(4-hydroxyphenyl)pyruvate, reduced 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)-3-(4-hydroxyphenyl)lactate:NAD(P)+ 2-oxidoreductase. Other names in common use include (R)-aromatic lactate dehydrogenase, and D-hydrogenase, D-aryllactate. This enzyme participates in tyrosine and phenylalanine catabolism.

References

  1. Enzyme 1.1.1.222 at KEGG Pathway Database.
  2. Bode R, Lippoldt A, Birnbaum D (1986). "Purification and properties of D-aromatic lactate dehydrogenase an enzyme involved in the catabolism of the aromatic amino acids of Candida maltosa". Biochem. Physiol. Pflanzen. 181 (3): 189–198. Bibcode:1986BioPP.181..189B. doi:10.1016/S0015-3796(86)80049-X.
  3. Leelayoova S, Marbury D, Rainey PM, Mackenzie NE, Hall JE (1992). "In vitro tryptophan catabolism by Leishmania donovani donovani promastigotes". J. Protozool. 39 (2): 350–8. doi:10.1111/j.1550-7408.1992.tb01329.x. PMID   1578411.