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βlactam antibiotics on L1 metal βlactamase stability and enzyme kinetics study
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βlactam antibiotics on L1 metal βlactamase stability and enzyme kinetics study
[Abstract] Objective To compare nine kinds of β lactam antibiotics on L1 metal β lactamase (metal enzyme) stability and the enzyme kinetic parameters, to understand the enzymatic properties of metal enzymes L1. Preparation of metal enzyme L1 of the purified product in order to ultraviolet spectrophotometer nine kinds of β lactam antibiotics on L1 metal enzyme stability and enzyme kinetic parameters. The results re-L1 enzymatic hydrolysis of penicillin and carbapenem antibiotics, the ability to close, aztreonam, and ceftazidime and a high degree of stability to the L1 enzyme. Conclusion L1 enzyme stability and kinetics of reasonable clinical application of antibiotics as a guide to provide a scientific theory.
[Keywords:] β lactam antibiotics; L1 metal enzyme; stability; enzyme kinetics
ABSTRACT Objective To investigate the stability of β lactams to L1 metallo β lactamase and its enzyme kinetic parameters. Methods The L1 fusion protein was expressed and purified from the recombinant E.coli. The stability and kinetic parameters of 9 β lactams to L1 were detected by spectrophotometer. Results Recombinant L1 showed the similar hydrolyzing capacity to penicillin and carbapenems, but highly stable against aztreonam and ceftazidime. Conclusion The stability and enzyme kinetics of 9 β lactams to L1 metallo β lactamase provided a guideline for the clinical use of antibiotics.
KEY WORDS β lactams; L1 metallo β lactamase; Stability; Enzyme kinetic
Stenotrophomonas maltophilia is a widow raising a kind of opportunistic pathogen that mainly affects the low immunity or long-term heavy use of broad-spectrum antibiotics. Bacteria is not common in clinical practice in the past, but over the past 10 years, infections caused by it gradually increased and has become an important pathogen of nosocomial infections in the clinical
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