Open AccessPurification and properties of the Mycobacterium smegmatis mc 2 155 β‐lactamase
Author(s) -
Quinting Birgit,
Galleni Moreno,
Timm Juliano,
Gicquel Brigitte,
Amicosante Gianfranco,
Frère JeanMarie
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb10301.x
Subject(s) - mycobacterium smegmatis , mycobacterium fortuitum , mycobacterium , microbiology and biotechnology , enzyme , chemistry , biology , biochemistry , bacteria , genetics , mycobacterium tuberculosis , medicine , tuberculosis , pathology
The β‐lactamase of Mycobacterium smegmatis mc 2 155 has been purified to protein homogeneity. Its N‐terminal sequence and catalytic properties are similar to those of the β‐lactamase produced by Mycobacterium fortuitum D316 and establish this new enzyme as a member of molecular class A.