Single substitution in amino acid composition between TEM-2 β-lactamase and a variant with altered kinetic constants
- 1 March 1983
- journal article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 17 (1-3) , 151-155
- https://doi.org/10.1111/j.1574-6968.1983.tb00391.x
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- Active sites of β-lactamases. The chromosomal β-lactamases of Pseudomonas aeruginosa and Escherichia coliBiochemical Journal, 1982
- .beta.-Lactamase proceeds via an acyl-enzyme intermediate. Interaction of the Escherichia coli RTEM enzyme with cefoxitinBiochemistry, 1980
- The structure of β-lactamasesPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1980
- Penicillinase active sites: Labelling of serine‐44 in β‐lactamase I by 6β‐bromopenicillanic acidFEBS Letters, 1979
- Directed selective pressure on a β-lactamase to analyse molecular changes involved in development of enzyme functionNature, 1976
- Etude cinétique de deux βlactamases responsables d'un même phénotypeBiochimie, 1974
- Maturation of the head of bacteriophage T4Journal of Molecular Biology, 1973
- Computerized microacidimetric determination of β lactamase Michaelis—Menten constantsFEBS Letters, 1973
- Structure and Mechanism of β-Lactamase from Escherichia coliBiochemical Society Transactions, 1973
- Analysis by Transduction of Mutations affecting Penicillinase Formation in Staphylococcus aureusJournal of General Microbiology, 1963