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• W2152164908 abstract "Abstract Pseudomonas fluorescens ATCC 948 expressed cell-associated peptidase activity, which was shown by subcellular fractionation to be primarily in the cytoplasmic fraction. An aminopeptidase of broad specificity was purified 129-fold over the crude extract with an 11% recovery by ion-exchange chromatography, biogel filtration, and affinity chromatography. The enzyme had a monomeric structure and a molecular weight of about 50,000. The optimal activity occurred at pH 7.5 and 45°C. A heat treatment of 75°C for 1min was necessary to inactivate the enzyme irreversibly. The aminopeptidase was strongly activated by Co 2+ , completely inhibited by EDTA and 1,10-phenanthroline, and weakly inhibited by sulfhydryl-blocking agent, suggesting that the aminopeptidase likely is a metalloenzyme with a thiol group at its active site. The enzyme showed high activity with β -naphthylamide derivatives that had a hydrophobic AA (Leu, Ala, or Phe) or diaminomonocarboxylic acid (Lys or Arg) at the N terminus. The occurrence of only one aminopeptidase active on Leu, Lys, or Arg aminoacyl bonds was demonstrated by the competitive inhibition of Lys- β -naphthylamide and Arg- β -naphthylamide on the activity against Leu- p -nitroanilide. Kinetic studies conducted on Leu- β -naphthylamide showed a Michaelis-Menton constant of .3m M , a maximum velocity of 10 nkat, and an energy of activation of 6200 cal/mol." @default.
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• W2152164908 date "1995-01-01" @default.
• W2152164908 modified "2023-09-26" @default.
• W2152164908 title "Purification and Characterization of Intracellular Aminopeptidase from Pseudomonas fluorescens ATCC 948" @default.
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• W2152164908 doi "https://doi.org/10.3168/jds.s0022-0302(95)76614-0" @default.
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