title: Purification and properties of the Mycobacterium smegmatis mc(2)155 beta-lactamase.
abstract: The beta-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 beta-lactamase produced by Mycobacterium fortuitum D316 and establish this new enzyme as a member of molecular class A.
authors.affiliation: Centre d'Ingénierie des Proteines, Université de Liège, Belgium.
authors.forename: B
authors.initials: B
authors.lastname: Quinting
authors.forename: M
authors.initials: M
authors.lastname: Galleni
authors.forename: J
authors.initials: J
authors.lastname: Timm
authors.forename: B
authors.initials: B
authors.lastname: Gicquel
authors.forename: G
authors.initials: G
authors.lastname: Amicosante
authors.forename: J M
authors.initials: JM
authors.lastname: Frère
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D019791:Guanidine; D006146:Guanidines; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008969:Molecular Sequence Data; D009161:Mycobacterium / Q000201:enzymology* / Q000235:genetics; D011489:Protein Denaturation; D017386:Sequence Homology, Amino Acid; D014508:Urea; D001618:beta-Lactamases / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D006146:Guanidines; D014508:Urea; D001618:beta-Lactamases; D019791:Guanidine