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Metabolic Modeling Tutorial
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Escherichia coli K-12 substr. MG1655 Reaction: 3.4.11.1

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: 3.4.11.1

Enzymes and Genes:
aminopeptidase A/I and DNA-binding transcriptional repressor Inferred from experiment : pepA

Supersedes EC number: 3.4.1.1

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

Summary:
This reaction is the hydrolysis of a peptide bond in a dipeptide. Substrates include cysteinylglycine.

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 3.4.1.1

Citations: [vanLoonKlaassen80, Suzuki01, Miller78a]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:3.4.11.1 , ENZYME:EC:3.4.11.1 , IUBMB-ExplorEnz:EC:3.4.11.1


References

Miller78a: 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 EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, BIOCYC13B.