title: Purification and characterization of aminopeptidase yspI from Schizosaccharomyces pombe.
abstract: Aminopeptidase yspI was purified to apparent homogeneity from the fission yeast Schizosaccharomyces pombe. The molecular mass of the native enzyme was estimated to be 184 kDa by gel filtration chromatography. A value of 92 kDa was calculated after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme is thus a dimer with two identical subunits. Optimum pH for cleavage of synthetic aminoacyl-4-nitroanilides is 7.0. Mercury ions, EDTA and chloroquine were found to be potent inhibitors of aminopeptidase yspI activity. Substrate specificity studies indicate that the purified enzyme cleaves L-lysine-4-nitroanilide with high efficiency.
authors.affiliation: Departamento de Biologia Funcional, Facultad de Medicina, Universidad de Oviedo, Spain.
authors.forename: M J
authors.initials: MJ
authors.lastname: Arbesú
authors.forename: E
authors.initials: E
authors.lastname: Valle
authors.forename: P
authors.initials: P
authors.lastname: Suárez-Rendueles
mesh_terms: D000595:Amino Acid Sequence; D000626:Aminopeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D002413:Cations, Divalent / Q000494:pharmacology; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012568:Schizosaccharomyces / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D002413:Cations, Divalent; D000626:Aminopeptidases; C082560:aminopeptidase yspI