MetaCyc Reaction:

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

EC Number:

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655: aminopeptidase A/I and DNA-binding transcriptional repressorInferred from experiment: pepA
Hordeum vulgare: barley leucine aminopeptidaseInferred from experiment
Rattus norvegicus: cysteinylglycinase / cytosolic leucyl aminopeptidaseInferred from experiment: LAP3
Solanum lycopersicum: acidic-leucine aminopeptidaseInferred from experiment: LAP-A2
acidic leucine aminopeptidaseInferred from experiment: LAP-A1
neutral leucine aminopeptidaseInferred from experiment: LAP-N

Supersedes 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.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: leucyl aminopeptidase

Enzyme Commission Synonyms: leucine aminopeptidase, leucyl peptidase, peptidase S, cytosol aminopeptidase, cathepsin III, L-leucine aminopeptidase, leucinaminopeptidase, leucinamide aminopeptidase, FTBL proteins, proteinates FTBL, aminopeptidase II, aminopeptidase III, aminopeptidase I

Standard Gibbs Free Energy (ΔrG in kcal/mol): -2.8899994Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Release of an N-terminal amino acid, XaaYaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low.

This is a zinc enzyme isolated from pig kidney and cattle lens; activated by heavy metal ions. Type example of peptidase family M17. Formerly EC

Citations: [vanLoonKlaassen80, Suzuki01, Miller78]

Gene-Reaction Schematic

Gene-Reaction Schematic

Instance reaction of [a [Cys-Gly]-S-conjugate + H2O → an L-cysteine-S-conjugate + glycine] (
i2: 4-hydroxy-2-nonenal-[Cys-Gly] conjugate + H2O → 4-hydroxy-2-nonenal-[L-Cys] conjugate + glycine (

Instance reaction of [a dipeptide + H2O → 2 amino acids] (
i1: L-glutamyl-L-glutamate + H2O → 2 L-glutamate (

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, UniProt:RELATED-TO:O24022, UniProt:RELATED-TO:P00727, UniProt:RELATED-TO:P23341, UniProt:RELATED-TO:P24828, UniProt:RELATED-TO:P27888, UniProt:RELATED-TO:P28839, UniProt:RELATED-TO:P30184, UniProt:RELATED-TO:P31427, UniProt:RELATED-TO:P45334, UniProt:RELATED-TO:P68767, UniProt:RELATED-TO:Q9JTI8, UniProt:RELATED-TO:Q9PP04, UniProt:RELATED-TO:Q10712, UniProt:RELATED-TO:Q42876, UniProt:RELATED-TO:Q43034, UniProt:RELATED-TO:Q48531


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

Miller78: Miller CG, Schwartz G (1978). "Peptidase-deficient mutants of Escherichia coli." J Bacteriol 135(2);603-11. PMID: 355237

Suzuki01: Suzuki H, Kamatani S, Kim ES, Kumagai H (2001). "Aminopeptidases A, B, and N and dipeptidase D are the four cysteinylglycinases of Escherichia coli K-12." J Bacteriol 183(4);1489-90. PMID: 11157967

vanLoonKlaassen80: van Loon-Klaassen LA, Cuypers HT, van Westreenen H, de Jong WW, Bloemendal H (1980). "The primary structure of bovine lens leucine aminopeptidase. Complete amino acid sequence of the N-terminal cyanogen bromide fragment and site of limited tryptic digestion." Biochem Biophys Res Commun 95(1);334-41. PMID: 7417261

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 Pathway Tools version 19.5 (software by SRI International) on Mon Nov 30, 2015, biocyc11.