CATH Classification

Domain Context

CATH Clusters

Functional Family

Enzyme Information
D-lactate dehydratase.
based on mapping to UniProt P31658
(R)-lactate = methylglyoxal + H(2)O.
-!- The enzyme, described from the fungi Candida albicans and Schizosaccharomyces pombe, converts 2-oxopropanal to (R)-lactate in a single glutathione (GSH)-independent step. -!- The other known route for this conversion is the two-step GSH- dependent pathway catalyzed by EC and EC
Thiolester hydrolases.
based on mapping to UniProt P31658
In linear amides.
based on mapping to UniProt P31658
Protein deglycase.
based on mapping to UniProt P31658
(1) An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H(2)O = a [protein]-L-arginine + lactate. (2) An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H(2)O = a [protein]-L-lysine + lactate. (3) An S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H(2)O = a [protein]-L-cysteine + lactate.
-!- 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.

UniProtKB Entries (1)

Escherichia coli K-12
Protein/nucleic acid deglycase 1

PDB Structure

PDB 1N57
External Links
Organism Escherichia
Primary Citation
The 1.6A Crystal Structure of the Class of Chaperone Represented by Escherichia coli Hsp31 Reveals a Putative Catalytic Triad
Quigley, P.M., Korotkov, K., Baneyx, F., Hol, W.G.J.