CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.50.880
Functional Family Protein/nucleic acid deglycase DJ-1

Enzyme Information

3.5.1.124
Protein deglycase.
based on mapping to UniProt Q99497
(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.
3.1.2.-
Thiolester hydrolases.
based on mapping to UniProt Q99497
3.5.1.-
In linear amides.
based on mapping to UniProt Q99497

UniProtKB Entries (1)

Q99497
PARK7_HUMAN
Homo sapiens
Protein/nucleic acid deglycase DJ-1

PDB Structure

PDB 3BWE
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of filamentous aggregates of human DJ-1 formed in an inorganic phosphate-dependent manner.
Cha, S.S., Jung, H.I., Jeon, H., An, Y.J., Kim, I.K., Yun, S., Ahn, H.J., Chung, K.C., Lee, S.H., Suh, P.G., Kang, S.O.
J.Biol.Chem.