Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
BRITE hierarchy

a [protein]-L-amino acid-1-hydroxypropan-2-one hydrolase [(R)-lactate-forming]

(1) an Nomega-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H2O = a [protein]-L-arginine + lactate [RN:R11562];
(2) an N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H2O = a [protein]-L-lysine + lactate [RN:R11563];
(3) an S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H2O = a [protein]-L-cysteine + lactate [RN:R11564]

R11562 R11563 R11564
Reaction

Nomega-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine;
H2O [CPD:C00001];
N6-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine;
S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine

The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively [3,4].

EC 3.5.1.124 created 2016