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- W2076601981 abstract "An aminopeptidase (APF1) with high specificity for phenylalanine and tyrosine in the active site P1 position was purified from mycelial extracts of the wood-decaying basidiomycete Schizophyllum commune. A two-dimensional preparative electrophoretic scheme resulted in a 60-fold purification of the enzyme, which was found to have an Mr of approximately 60 kDa by size exclusion chromatography. SDS-PAGE resolved two closely migrating subunits of approximately 30 and 31 kDa. Its pi was found to be 5·5 and its activity optimum was pH 6·5. Of 11 aminoacyl-p-nitroanilide (-pNA) substrates tested, activity was found only against Phe-pNA. APF1 also showed activity against Phe-β-naphthylamide (-βNA) and Tyr-βNA; however, the activity against Tyr-βNA was less than one third of that against Phe-βNA. No other AA-βNA substrates were hydrolysed. APF1 hydrolysed a variety of dipeptides with Phe in the P1 position; the amino acid in the P′1 position affected the rate. No activity was found against dipeptides where Phe was not the N-terminus nor against substrates that were N-blocked. APF1 was partially inhibited by 1,10-phenanthroline, and this inhibition was reversible by the addition of Zn2+." @default.
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- W2076601981 date "1996-04-01" @default.
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- W2076601981 title "Characterization of a novel phenylalanine-specific aminopeptidase from Schizophyllum commune" @default.
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- W2076601981 doi "https://doi.org/10.1016/s0953-7562(96)80144-4" @default.
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