β-Lactamases from Yersinia enterocolitica Free

Abstract

SUMMARY: Two -lactamases, A and B, have been shown to be present in a strain of (W222). -Lactamase A hydrolyses a variety of penicillins and cephalosporins. This enzyme is sensitive to thiol reagents, is only partially inhibited 0·1 m-cloxacillin and has a molecular weight of approximately 20000. -Lactamase B shows strong cephalosporinase activity but does not hydrolyse some of the penicillins. It is more resistant than -lactamase A to thiol reagents, is completely inhibited 0·1 m-cloxacillin and has a molecular weight of about 34000. With cephaloridine as a substrate, which is readily hydrolysed both enzymes, about 85% of the total activity of a cell extract is due to -lactamase A and 15% to B. Addition of 6-aminopenicillanic acid to the culture during growth results in a 2- to 4-fold selective increase in the amount of -lactamase B. Two -lactamases similar to enzymes A and B have been found in five other strains of In contrast, only one -lactamase, similar to enzyme B, has been detected in a different strain of (H66), which is abnormal in that it is sensitive to ampicillin. Addition of 6-aminopenicillanic acid to cultures of this strain results in an 8- to 10-fold increase in -lactamase production.

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1975-04-01
2024-03-28
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