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 6F2F
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Unveiling the Binding Modes of the Crystallophore, a Terbium-based Nucleating and Phasing Molecular Agent for Protein Crystallography.
Engilberge, S., Riobe, F., Wagner, T., Di Pietro, S., Breyton, C., Franzetti, B., Shima, S., Girard, E., Dumont, E., Maury, O.
Chemistry