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Escherichia coli K-12 substr. MG1655 Reaction: 3.4.13.18


Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 3.4.13.18

Enzymes and Genes:
peptidase DInferred from experiment: pepD

Supersedes EC numbers: 3.4.3.6, 3.4.3.2, 3.4.3.1, 3.4.13.15, 3.4.13.8, 3.4.13.2, 3.4.13.1

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Mass balance status: Balanced.

Enzyme Commission Primary Name: cytosol nonspecific dipeptidase

Enzyme Commission Synonyms: N2-β-alanylarginine dipeptidase, glycyl-leucine dipeptidase, peptidase A, Pro-X dipeptidase, prolyl dipeptidase, iminodipeptidase, prolinase, L-prolylglycine dipeptidase, prolylglycine dipeptidase, diglycinase, Gly-Leu hydrolase, glycyl-L-leucine dipeptidase, glycyl-L-leucine peptidase, L-amino-acyl-L-amino-acid hydrolase, glycylleucine peptidase, glycylleucine hydrolase, glycylleucine dipeptide hydrolase, non-specific dipeptidase, human cytosolic non-specific dipeptidase, glycyl-L-leucine hydrolase, glycyl-glycine dipeptidase

Enzyme Commission Summary:
This enzyme catalyzes the hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids. It is a zinc enzyme with broad specificity, varying somewhat with source species. Activated and stabilized by dithiothreitol and Mn2+. Inhibited by bestatin and leucine.

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:3.4.13.18, ENZYME:EC:3.4.13.18, IUBMB-ExplorEnz:EC:3.4.13.18


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by Pathway Tools version 19.5 (software by SRI International) on Fri Feb 12, 2016, biocyc14.