Protein/nucleic acid deglycase DJ-1 (IPR006287)

Short name: DJ-1

Overlapping homologous superfamilies

Family relationships



Glycation is a nonenzymatic covalent reaction between proteins and endogenous reducing sugars or dicarbonyls (methylglyoxal, glyoxal) that results in protein inactivation. DJ-1 was described in vitro as a protein deglycase that repaired methylglyoxal- and glyoxal-glycated proteins [PMID: 25416785, PMID: 26995087]. Since then there have been reports against [PMID: 27903648], and supporting this role for DJ-1 [PMID: 28013050]. Furthermore, supporting its deglycase activity, DJ-1 and its bacterial homologues have been shown to be able to repair methylglyoxal- and glyoxal-glycated nucleotides and nucleic acids [PMID: 28596309]. This ability would make DJ-1 a target for diabetic and cancer research [PMID: 28706026]. DJ-1, also known as Park7, has been associated with human parkinsonism [PMID: 12446870].

Included in this family is also YajL from Escherichia coli, the bacterial homologue of DJ-1 [PMID: 20889753, PMID: 26774339]. This group of proteins are classified as either DJ-1 putative peptidases or non-peptidase homologues in MEROPS peptidase family C56 (clan PC(C)).

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.