Abstract
The beta-lactamases of Streptomyces albus G and Actinomadura R39 are inactivated by beta-iodopenicillanate. However, in contrast with the beta-lactamase I from Bacillus cereus, they also efficiently catalyse the hydrolysis of the inactivator; with the S. albus G enzyme, kcat. is larger than 25s-1 and the number of turnovers before inactivation is 515. With the A. R39 enzyme, kcat. is larger than 50s-1 and the number of turnovers before inactivation is 80. After hydrolysis of the beta-lactam amide bond, the product rearranges into 2.3-dihydro-2,2-dimethyl-1,4-thiazine-3,6-dicarboxylate, which exhibits an absorption maximum at 305 nm.
MeSH Terms
Actinomycetaceae/enzymology
Hydrolysis
Kinetics
Mass Spectrometry
Models, Biological
Penicillanic Acid/metabolism
Streptomyces/enzymology
beta-Lactamase Inhibitors
Chemicals
beta-Lactamase Inhibitors
Penicillanic Acid
6-iodopenicillanic acid
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Frère J M
Dormans C
Duyckaerts C
De Graeve J
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