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 6Q3T
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
A simple and versatile microfluidic device for efficient biomacromolecule crystallization and structural analysis by serial crystallography.
de Wijn, R., Hennig, O., Roche, J., Engilberge, S., Rollet, K., Fernandez-Millan, P., Brillet, K., Betat, H., Morl, M., Roussel, A., Girard, E., Mueller-Dieckmann, C., Fox, G.C., Olieric, V., Gavira, J.A., Lorber, B., Sauter, C.
Iucrj