Characterization of a β-lactamase produced in Mycobacterium fortuitum D316
Keyword(s):
Class A
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A beta-lactamase from Mycobacterium fortuitum D316 was purified and some physico-chemical properties and substrate profile determined. On the basis of its N-terminal sequence and of its sensitivity to beta-iodopenicillanate inactivation, the enzyme appeared to be a class A beta-lactamase, but its substrate profile was quite unexpected, since nine cephalosporins were among the eleven best substrates. The enzyme also hydrolysed ureidopenicillins and some so-called ‘beta-lactamase-stable’ cephalosporins.
2018 ◽
Vol 808
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pp. 266-277
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2019 ◽
Vol 558
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pp. 341-350
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2004 ◽
Vol 22
(9-10)
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pp. 1199-1211
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Keyword(s):
2019 ◽
Vol 18
(2)
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pp. 274-284
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Keyword(s):
Keyword(s):
2011 ◽
Vol 89
(3)
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pp. 335-340
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Keyword(s):
2011 ◽
Vol 236-238
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pp. 538-542