|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: 220.127.116.11
Enzymes and Genes:
aminopeptidase A/I and DNA-binding transcriptional repressor : pepA
Supersedes EC number: 18.104.22.168
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
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 22.214.171.124
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
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