The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 3.4.11.1     
Accepted name: leucyl aminopeptidase
Reaction: Release of an N-terminal amino acid, Xaa┼Yaa-, 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
Other name(s): 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
Comments: A zinc enzyme isolated from pig kidney and cattle lens; activated by heavy metal ions. Type example of peptidase family M17.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9001-61-0
References:
1.  Himmelhoch, S.R. Leucine aminopeptidase from swine kidney. Methods Enzymol. 19 (1970) 508–513.
2.  Delange, R.J. and Smith, E.L. Leucine aminopeptidase and other N-terminal exopeptidases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 3, Academic Press, New York, 1971, pp. 81–118.
3.  van Loon-Klaasen, L.A.H., Cuypers, H.T., van Westreenen, H., de Jong, W.W. and Bloemendal, H. The primary structure of bovine lens leucine aminopeptidase. Complete amino acid sequence of the N-terminal cyanogen bromide fragment and site limited tryptic digestion. Biochem. Biophys. Res. Commun. 95 (1980) 334–341. [DOI] [PMID: 7417261]
[EC 3.4.11.1 created 1961 as EC 3.4.1.1, transferred 1972 to EC 3.4.11.1]
 
 


Data © 2001–2024 IUBMB
Web site © 2005–2024 Andrew McDonald