The Enzyme Database

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EC 3.4.13.23     
Accepted name: cysteinylglycine-S-conjugate dipeptidase
Reaction: an [L-cysteinylglycine]-S-conjugate + H2O = an L-cysteine-S-conjugate + glycine
Other name(s): tpdA (gene name); LAP3 (gene name)
Systematic name: cysteinylglycine-S-conjugate dipeptide hydrolase
Comments: The enzyme participates in a widespread glutathione-mediated detoxification pathway. In animals the activity is usually catalysed by enzymes that have numerous additional activities, such as EC 3.4.11.1, leucyl aminopeptidase, EC 3.4.11.2, membrane alanyl aminopeptidase, and EC 3.4.13.19, membrane dipeptidase. However, in the bacterium Corynebacterium sp. Ax20, which degrades axillary secretions, the enzyme appears to be specific for this task.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  SEMENZA G Chromatographic purification of cysteinyl-glycinase. Biochim. Biophys. Acta 24 (1957) 401–413. [PMID: 13436444]
2.  Rankin, B.B., McIntyre, T.M. and Curthoys, N.P. Brush border membrane hydrolysis of S-benzyl-cysteine-p-nitroanilide, and activity of aminopeptidase M. Biochem. Biophys. Res. Commun. 96 (1980) 991–996. [PMID: 6108111]
3.  Hirota, T., Nishikawa, Y., Takahagi, H., Igarashi, T. and Kitagawa, H. Simultaneous purification and properties of dehydropeptidase-I and aminopeptidase-M from rat kidney. Res Commun Chem Pathol Pharmacol 49 (1985) 435–445. [PMID: 2865778]
4.  Josch, C., Klotz, L.O. and Sies, H. Identification of cytosolic leucyl aminopeptidase (EC 3.4.11.1) as the major cysteinylglycine-hydrolysing activity in rat liver. Biol. Chem. 384 (2003) 213–218. [PMID: 12675513]
5.  Emter, R. and Natsch, A. The sequential action of a dipeptidase and a β-lyase is required for the release of the human body odorant 3-methyl-3-sulfanylhexan-1-ol from a secreted Cys-Gly-(S) conjugate by Corynebacteria. J. Biol. Chem. 283 (2008) 20645–20652. [PMID: 18515361]
[EC 3.4.13.23 created 2019]
 
 


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