Article
Characterization of a beta-lactamase produced in Mycobacterium fortuitum D316.
The Biochemical journal - 1 Nov 1990
Amicosante G, Franceschini N, Segatore B, Oratore A, Fattorini L, Orefici G, Van Beeumen J, Frere J M
Abstract excerpt
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...
Topics
- Amino Acid Sequence
- Amino Acids
- Bacterial Proteins
- Edetic Acid
- Hydroxymercuribenzoates
- Isoelectric Point
- Kinetics
- Molecular Sequence Data
- Molecular Weight
- Mutation
- Mycobacterium
- Nitrilotriacetic Acid
- Substrate Specificity
- beta-Lactamases