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- W2000364515 abstract "The chemical modification of purified ampicillin acylase by N-bromosuccinimide and diethylpyrocarbonate resulted in time-dependent inactivation of the enzyme. Both substrates, ampicillin and 6-aminopenicillanic acid, protected the enzyme against inactivation, suggesting that the modification occurred near or at the active site. Amino acid analyses and other data indicated that two histidyl residues per subunit molecule were essential for catalytic activity." @default.
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- W2000364515 title "Evidence for involvement of 2 histidine residues in the reaction of ampicillin acylase" @default.
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- W2000364515 doi "https://doi.org/10.1016/0006-291x(90)90896-u" @default.
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