Zinc-dependent aminopeptidases: new perspectives on structure, function, and biomedical applications
Frontiers in Chemical BiologyZinc-dependent aminopeptidases are a subclass of exopeptidases implicated in the hydrolysis of N-terminal residues from peptides through a Zn(II) co-factor dependent hydrolytic mechanism. In humans, the prominent members of this class of enzymes (ERAP1/2,
Saleem Bhat
doaj +1 more source
Structural Basis for Catalysis by the Mono- and Dimetalated Forms of the \u3cem\u3edapE\u3c/em\u3e-Encoded \u3cem\u3eN\u3c/em\u3e-succinyl-L,L-Diaminopimelic Acid Desuccinylase [PDF]
, 2010 Biosynthesis of lysine and meso-diaminopimelic acid in bacteria provides essential components for protein synthesis and construction of the bacterial peptidoglycan cell wall. The dapE operon enzymes synthesize both meso-diaminopimelic acid and lysine and,
Fan, Yao +4 more
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Inhibition of the Aminopeptidase from \u3cem\u3eAeromonas proteolytica\u3c/em\u3e by l-leucinethiol: Kinetic and Spectroscopic Characterization of a Slow, Tight-binding Inhibitor–enzyme Complex [PDF]
, 2000 The peptide inhibitor l-leucinethiol (LeuSH) was found to be a potent, slow-binding inhibitor of the aminopeptidase from Aeromonas proteolytica (AAP). The overall potency (KI*) of LeuSH was 7 nM while the corresponding alcohol l-leucinol (LeuOH) was a ...
Bennett, Brian +2 more
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Mutation of H63 and its Catalytic Affect on the Methionine Aminopeptidase from \u3cem\u3eEscherichia coli\u3c/em\u3e [PDF]
, 2009 In order to gain insight into the mechanistic role of a flexible exterior loop near the active site, made up of Y62, H63, G64, and Y65, that has been proposed to play an important role in substrate binding and recognition in the methionyl aminopeptidase ...
Bennett, Brian +2 more
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ETEC colonisation factors disrupt the antigen presenting capacity of porcine intestinal dendritic cells [PDF]
, 2012 Enterotoxigenic E. coli (ETEC) are not only a major cause of diarrhoea in travellers to and children in developing countries, but also cause neonatal and postweaning diarrhoea in piglets, leading to a reduced feed conversion and a higher mortality rate ...
Baert, Kim, Devriendt, Bert, Luo, Yu
core
Function of the Signal Peptide and N- and C-terminal Propeptides in the Leucine Aminopeptidase from \u3cem\u3eAeromonas proteolytica\u3c/em\u3e [PDF]
, 2004 The leucine aminopeptidase from Aeromonas proteolytica (also known as Vibrio proteolyticus) (AAP) is a metalloenzyme with broad substrate specificity. The open reading frame (ORF) for AAP encodes a 54 kDa enzyme, however, the extracellular enzyme has a ...
Bzymek, Krzysztof P. +5 more
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Leucine Aminopeptidase to Spleen Length Ratio: A Novel Noninvasive Model for Predicting Esophageal Gastric Variceal Bleeding in Patients With Liver Cirrhosis. [PDF]
Gastroenterol Res PractZhu C, Jiang Y, Liu Y, Bian Z, Luo L.
europepmc +1 more source
Aminopeptidase M17 in bacteria: insights into structure, function, and potential as a drug target. [PDF]
J BacteriolAskar H +7 more
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Safety evaluation of the food enzyme leucyl aminopeptidase from the non-genetically modified <i>Lichtheimia ramosa</i> strain AE-PER. [PDF]
EFSA JEFSA Panel on Food Enzymes (FEZ) +17 more
europepmc +1 more source
Safety evaluation of an extension of use of the food enzyme leucyl aminopeptidase from the non-genetically modified <i>Lichtheimia ramosa</i> strain AE-PER. [PDF]
EFSA JEFSA Panel on Food Enzymes (FEZ) +14 more
europepmc +1 more source