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ends Feb 21th, 2015
Metabolic Modeling Tutorial
early discounted registration
ends Feb 21th, 2015

MetaCyc Reaction:

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:

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

In Pathway: wound-induced proteolysis I , seed germination protein turnover

Supersedes EC number:

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Undetermined; a substrate lacks a chemical formula

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

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, Suzuki01a, Miller78]

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


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

Suzuki01a: 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 SRI International Pathway Tools version 18.5 on Mon Mar 2, 2015, biocyc14.