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• W1969902013 abstract "Penicillin acylase from Alcaligenes faecalis has a very high affinity for both natural (benzylpenicillin, K m =0.0042 mM) and colorimetric (6‐nitro‐3‐phenylacetamidobenzoic acid, K m =0.0045 mM) substrates as well as the product of their hydrolysis, phenylacetic acid ( K i =0.016 mM). The enzyme is partially inhibited at high benzylpenicillin concentrations but the triple SES complex formed still retains 43% of the maximal catalytic activity; the affinity of benzylpenicillin for the second substrate molecule binding site is much lower ( K S ′=54 mM) than for the first one. Phenylmethylsulfonyl fluoride was shown to be a very effective irreversible inhibitor, completely inactivating the penicillin acylase from A. faecalis in a few minutes at micromolar concentrations; this compound was used for enzyme active site titration. The absolute values of the determined kinetic parameters for enzymatic hydrolysis of 6‐nitro‐3‐phenylacetamidobenzoic acid ( k cat =95 s −1 and k cat / K m =2.1×10 −7 M −1 s −1 ) and benzylpenicillin ( k cat =54 s −1 and k cat / K m =1.3×10 −7 M −1 s −1 ) by penicillin acylase from A. faecalis were shown to be highest of all the enzymes of this family that have so far been studied." @default.
• W1969902013 created "2016-06-24" @default.
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• W1969902013 date "1997-11-17" @default.
• W1969902013 modified "2023-09-25" @default.
• W1969902013 title "Kinetic study of penicillin acylase from <i>Alcaligenes faecalis</i>" @default.
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• W1969902013 doi "https://doi.org/10.1016/s0014-5793(97)01289-1" @default.
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