A β-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 β-iodopenicillanate inactivation, the enzyme appeared to be a class A β-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 'β-lactamase-stable' cephalosporins.
|Titolo:||Characterization of a β-lactamase produced in Mycobacterium fortuitum D316|
|Data di pubblicazione:||1990|
|Appare nelle tipologie:||1.1 Articolo in rivista|