Use of electrospray mass spectrometry to investigate the inhibition of β-lactamases by 6-halogenopenicillanic acids
- 1 January 1993
- journal article
- research article
- Published by Royal Society of Chemistry (RSC) in Journal of the Chemical Society, Chemical Communications
- No. 2,p. 121-123
- https://doi.org/10.1039/c39930000121
Abstract
Electrospray mass spectrometry has been used to investigate the mechanism of inhibition of class A and C β-lactamases by 6-halogenopenicillanic acids; in the case of the 6β-halogen substituted penicillanic acids the molecular mass differences observed between the unreacted and the inhibited β-lactamases are consistent with the formation of an enzyme bound dihydrothiazine derivative, as previously proposed.Keywords
This publication has 10 references indexed in Scilit:
- Use of electrospray mass spectrometry to directly observe an acyl enzyme intermediate in β‐lactamase catalysisFEBS Letters, 1990
- New developments in biochemical mass spectrometry: electrospray ionizationAnalytical Chemistry, 1990
- Electrospray Ionization for Mass Spectrometry of Large BiomoleculesScience, 1989
- Inactivation of Bacillus cereus .beta.-lactamase I by 6.beta.-bromopenicillanic acid: mechanismBiochemistry, 1980
- Inactivation of Bacillus cereus .beta.-lactamase I by 6.beta.-bromopenicillanic acid: kineticsBiochemistry, 1980
- On the chemistry of β-lactamase inhibition by 6β-bromopenicillanic acidJournal of the Chemical Society, Perkin Transactions 1, 1980
- 6 β-Bromopenicillanic acid inactivates β-lactamase IBiochemical Journal, 1979
- 6-beta-bromopenicillanic acid, a potent beta-lactamase inhibitor.Proceedings of the National Academy of Sciences, 1978
- The partial amino acid sequence of the extracellular β-lactamase I of Bacillus cereus 569/HBiochemical Journal, 1975
- Separation, purification and properties of β-lactamase I and β-lactamase II from Bacillus cereus 569/H/9Biochemical Journal, 1974