Aromatic 2-oxoacid reductase

Enzyme From Wikipedia, the free encyclopedia

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.

2D representation of the chemical structure of Q27098335.
(R)-3-(4-hydroxyphenyl)lactate
 
 
 
H+
Reversible left-right reaction arrow with minor forward product(s) to top right and minor reverse substrate(s) from bottom right
 
H+
 
2D representation of the chemical structure of Q2823224.
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

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