A Reversible Inhibitor of P-Lactamase I from Bacillus cereus

Mark Jones; Stephen C. Buckwell; Michael I. Page; Roger Wrigglesworth

doi:10.1039/C39890000070

A Reversible Inhibitor of P-Lactamase I from Bacillus cereus

Mark Jones, Stephen C. Buckwell, Michael I. Page, Roger Wrigglesworth

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5 Citations (Scopus)

Abstract

α-Methyl (3S,5R,6R)benzylpenicilloate is a reversible competitive inhibitor of β-lactamase l from Bacillus cereus; the inhibition constant K_i is 6.38 × 10^-4M and is independent of pH between pH 5 and 8 which is compatible with binding of the free base form of the thiazolidine residue to the enzyme.

Original language	English
Pages (from-to)	70-71
Number of pages	2
Journal	Journal of the Chemical Society, Chemical Communications
Issue number	2
DOIs	https://doi.org/10.1039/C39890000070
Publication status	Published - Jan 1989

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Jones, M., Buckwell, S. C., Page, M. I., & Wrigglesworth, R. (1989). A Reversible Inhibitor of P-Lactamase I from Bacillus cereus. Journal of the Chemical Society, Chemical Communications, (2), 70-71. https://doi.org/10.1039/C39890000070

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abstract = "α-Methyl (3S,5R,6R)benzylpenicilloate is a reversible competitive inhibitor of β-lactamase l from Bacillus cereus; the inhibition constant Ki is 6.38 × 10-4M and is independent of pH between pH 5 and 8 which is compatible with binding of the free base form of the thiazolidine residue to the enzyme.",

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AB - α-Methyl (3S,5R,6R)benzylpenicilloate is a reversible competitive inhibitor of β-lactamase l from Bacillus cereus; the inhibition constant Ki is 6.38 × 10-4M and is independent of pH between pH 5 and 8 which is compatible with binding of the free base form of the thiazolidine residue to the enzyme.

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10.1039/C39890000070

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