DPEPs hydrolyse glycine from AFXBO-CG, AFNBO-CG

Stable Identifier
R-HSA-5433067
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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In the formation of mercapturic acid from glutathione conjugates, first a glutamate residue is hydrolysed from the conjugate then a glycine residue (Gly). The dipeptidases 1,2 and 3 (DPEP1,2,3) perform this second hydrolysis. They are membrane-bound, homodimeric enzymes which require zinc ions for activity. DPEP1 has been characterised (Satoh et al. 1993, 1994, Nitanai et al. 2002) whereas DPEP2 and 3 are thought to function as DPEP1 based on similarity.

Literature References
PubMed ID Title Journal Year
8439558 Cloning and structural analysis of genomic DNA for human renal dipeptidase

Satoh, S, Kusunoki, C, Konta, Y, Niwa, M, Kohsaka, M

Biochim. Biophys. Acta 1993
12144777 Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis

Nitanai, Y, Satow, Y, Adachi, H, Tsujimoto, M

J. Mol. Biol. 2002
7764673 Gene structural analysis and expression of human renal dipeptidase

Satoh, S, Ohtsuka, K, Keida, Y, Kusunoki, C, Konta, Y, Niwa, M, Kohsaka, M

Biotechnol. Prog. 1994
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
dipeptidase activity of DPEP1,2,3 dimers [plasma membrane]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created