Characterization of a beta-lactamase produced in Mycobacterium fortuitum D316.
A beta-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 beta-iodopenicillanate inactivation, the enzyme appeared to be a class A beta-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 'beta-lactamase-stable' cephalosporins.
Amicosante
G
G
Università degli Studi dell'Aquila, Dipartimento di Scienze e Tecnologie Biomediche e Biometria, L'Aquila, Italy.
Franceschini
N
N
Segatore
B
B
Oratore
A
A
Fattorini
L
L
Orefici
G
G
Van Beeumen
J
J
Frere
J M
JM
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D004492:Edetic Acid / Q000494:pharmacology; D006902:Hydroxymercuribenzoates / Q000494:pharmacology; D007526:Isoelectric Point; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009154:Mutation; D009161:Mycobacterium / Q000201:enzymology* / Q000235:genetics; D009571:Nitrilotriacetic Acid / Q000494:pharmacology; D013379:Substrate Specificity; D001618:beta-Lactamases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
D000596:Amino Acids; D001426:Bacterial Proteins; D006902:Hydroxymercuribenzoates; C030601:4-hydroxymercuribenzoate; D004492:Edetic Acid; D001618:beta-Lactamases; D009571:Nitrilotriacetic Acid