Purification and properties of the Mycobacterium smegmatis mc(2)155 beta-lactamase.
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.
Quinting
B
B
Centre d'Ingénierie des Proteines, Université de Liège, Belgium.
Galleni
M
M
Timm
J
J
Gicquel
B
B
Amicosante
G
G
Frère
J M
JM
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*
D001426:Bacterial Proteins; D006146:Guanidines; D014508:Urea; D001618:beta-Lactamases; D019791:Guanidine