MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number:

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: Marked as unbalanced.

Enzyme Commission Primary Name: Xaa-Trp aminopeptidase

Enzyme Commission Synonyms: aminopeptidase W, aminopeptidase X-Trp, X-Trp aminopeptidase

Standard Gibbs Free Energy (ΔrG): -48.12524 kcal/molInferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Release of a variety of N-terminal residues (especially glutamate and leucine) from peptides, provided tryptophan (or at least phenylalanine or tyrosine) is the penultimate residue. Also acts on GluTrp, LeuTrp and a number of other dipeptides.

This is a glycoprotein containing Zn2+, from renal and intestinal brush border membranes.

Citations: [Gee85, Gee87]

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


Gee85: Gee NS, Kenny AJ (1985). "Proteins of the kidney microvillar membrane. The 130 kDa protein in pig kidney, recognized by monoclonal antibody GK5C1, is an ectoenzyme with aminopeptidase activity." Biochem J 230(3);753-64. PMID: 4062876

Gee87: Gee NS, Kenny AJ (1987). "Proteins of the kidney microvillar membrane. Enzymic and molecular properties of aminopeptidase W." Biochem J 246(1);97-102. PMID: 2890346

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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