Aromatic 2-oxoacid reductase
| indolelactate dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.1.110 | ||||||||
| CAS no. | 37250-41-2 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, an aromatic 2-oxoacid reductase (EC 1.1.1.110, previously indolelactate dehydrogenase) is an enzyme that catalyzes the reversible oxidation and reduction of aryllactate compounds to arylpyruvate compounds using the redox cofactor nicotinamide adenine dinucleotide or the similar nicotinamide adenine dinucleotide phosphate.[1][2][3][4] For example, the enzyme may oxidize (R)-3-(4-hydroxyphenyl)lactate to 3-(4-hydroxyphenyl)pyruvic acid.
This enzyme[5] is an oxidoreductase, oxidizing the CH-OH alcohol group to a carbonyl group. NAD+ is the oxidizing agent, yielding reduced NADH.
Aryllactates and arylpyruvates are intermediates in tyrosine, phenylalanine and tryptophan metabolism and blood serum levels of these compounds affect intestinal permeability and systemic immunity in mice.[4]
Alternative names for these enzymes are: (R)-aromatic lactate dehydrogenase, D-aryllactate D-hydrogenase, (indol-3-yl)lactate:NAD+ oxidoreductase, indolelactate:NAD+ oxidoreductase, (R)-4-hydroxyphenyllactate dehydrogenase, (R)-3-(4-hydroxyphenyl)lactate:NAD(P)+ 2-oxidoreductase
References
- ^ Jean M, DeMoss RD (1968). "Indolelactate dehydrogenase from Clostridium sporogenes". Can. J. Microbiol. 14 (4): 429–35. doi:10.1139/m68-068. PMID 4384683.
- ^ 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.
- ^ 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.
- ^ a b Dodd, Dylan; Spitzer, Matthew H.; Van Treuren, William; Merrill, Bryan D.; Hryckowian, Andrew J.; Higginbottom, Steven K.; Le, Anthony; Cowan, Tina M.; Nolan, Garry P.; Fischbach, Michael A.; Sonnenburg, Justin L. (2017). "A gut bacterial pathway metabolizes aromatic amino acids into nine circulating metabolites". Nature. 551 (7682): 648–652. doi:10.1038/nature24661. ISSN 1476-4687. PMC 5850949. PMID 29168502.
- ^ Enzyme 1.1.1.110 at KEGG Pathway Database.