Leucyl aminopeptidase - Wikipedia
For LAP-A, R1 could be the R group of leucine, methionine, or arginine. bovine lens LAP and PepA have been elucidated (Ref 1 and 2), however, the exact mechanism of tomato LAP-A is unknown at this time.
Leucine aminopeptidases: diversity in structure and function
Leucine aminopeptidases (LAPs) are metallopeptidases that cleave N-terminal residues from proteins and peptides. While hydrolyzing Leu substrates, LAPs often have a broader specificity. LAPs are members of the M1 or M17 peptidase families, and therefore the LAP nomenclature is …
Leucine aminopeptidases: diversity in structure and function - De …
2006年12月1日 · Leucine aminopeptidases (LAPs) are metallopeptidases that cleave N-terminal residues from proteins and peptides. While hydrolyzing Leu substrates, LAPs often have a broader specificity. LAPs are members of the M1 or M17 peptidase families, and therefore the LAP nomenclature is complex.
Leucine aminopeptidases: Diversity in structure and function
2007年1月1日 · Leucine aminopeptidases (LAPs) are metallopeptidases that cleave N-terminal residues from proteins and peptides. While hydrolyzing Leu substrates, LAPs often have a broader specificity. LAPs...
Aminopeptidases: structure and function - PubMed
1993年2月1日 · Crystallographic, electron micrographic, NMR, and photoaffinity labeling studies indicate that lens leucine aminopeptidase protomers are bilobal and that bestatin and substrates are bound in an active site, which is found in the larger lobe on each protomer.
Leucyl Aminopeptidase - an overview | ScienceDirect Topics
2011年3月4日 · Leucine aminopeptidase is a proteolytic enzyme that hydrolyzes amino acids, particularly leucine, from the N-terminus of proteins and polypeptides. At least in humans, it is widely distributed in tissues; however, activity is highest in …
Leucine aminopeptidases: diversity in structure and function
2006年12月1日 · Leucine aminopeptidases that cleave N-terminal residues from proteins and peptides are found to serve as transcriptional repressors to control pyrimidine, alginate and cholera toxin biosynthesis, as well as mediate site-specific recombination events in …
Leucine Aminopeptidase Activity - The New England Journal of Medicine
LEUCINE aminopeptidase is a proteolytic enzyme that is capable of hydrolyzing L-leucyl peptides. It is widely distributed in bacteria, plants and animals and has been demonstrated...
ENZYME - 3.4.11.1 leucyl aminopeptidase - Expasy
2011年3月4日 · leucyl aminopeptidase Alternative Name(s) cytosol aminopeptidase: leucine aminopeptidase: peptidase S: Reaction catalysed; 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.
Leucyl Aminopeptidase - an overview | ScienceDirect Topics
Leucine aminopeptidase, a Zn2+-containing enzyme, is an integral transmembrane glycoprotein with a carbohydrate-rich hydrophilic portion and active site protruding into the luminal side. You might find these chapters and articles relevant to this topic.