DPEPs hydrolyse glycine from AFXBO-CG, AFNBO-CG

Stable Identifier
R-HSA-5433067
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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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
12144777 Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis

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

J. Mol. Biol. 2002
8439558 Cloning and structural analysis of genomic DNA for human renal dipeptidase

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

Biochim. Biophys. Acta 1993
7764673 Gene structural analysis and expression of human renal dipeptidase

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

Biotechnol. Prog. 1994
Participants
Participates
Catalyst Activity

dipeptidase activity of DPEP1,2,3 dimers [plasma membrane]

Orthologous Events
Authored
Reviewed
Created
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