CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.50.880
Functional Family

Enzyme Information

3.4.22.-
Cysteine endopeptidases.
based on mapping to UniProt O59413
3.5.1.124
Protein deglycase.
based on mapping to UniProt O59413
(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)

O59413
DEGLY_PYRHO
Pyrococcus horikoshii OT3
Deglycase PH1704

PDB Structure

PDB 1G2I
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of an intracellular protease from Pyrococcus horikoshii at 2-A resolution.
Du, X., Choi, I.G., Kim, R., Wang, W., Jancarik, J., Yokota, H., Kim, S.-H.
Proc.Natl.Acad.Sci.USA