Purification and properties of the Mycobacterium smegmatis mc2155 β-lactamase

Purification and properties of the Mycobacterium smegmatis mc2155 β-lactamase

Abstract The β-lactamase of Mycobacterium smegmatis mc2155 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.

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Veröffentlicht in:FEMS microbiology letters 1997-04, Vol.149 (1), p.11-15
Hauptverfasser: Quinting, Birgit, Galleni, Moreno, Timm, Juliano, Gicquel, Brigitte, Amicosante, Gianfranco, Frère, Jean-Marie
Format: Artikel
Sprache:eng
Schlagworte:
Amino acid sequence
Microbiology
Mycobacterium smegmatis
Mycobacterium smegmatis mc2155 β‐lactamase
Purification
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Zusammenfassung:Abstract The β-lactamase of Mycobacterium smegmatis mc2155 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.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1997.tb10301.x