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MetaCyc Reaction: 3.4.11.16

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 3.4.11.16

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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 in kcal/mol): -48.12524 Inferred 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:3.4.11.16 , ENZYME:EC:3.4.11.16 , IUBMB-ExplorEnz:EC:3.4.11.16


References

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."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Fri Aug 28, 2015, biocyc12.