Characterization of covalently bound enzyme inhibitors as transition-state analogs by protein stability measurements: Phosphonate monoester inhibitors of .beta.-lactamase-Reference-Cited by-同舟云学术

Characterization of covalently bound enzyme inhibitors as transition-state analogs by protein stability measurements: Phosphonate monoester inhibitors of .beta.-lactamase

Published:1994-01-11 Issue:1 Volume:33 Page:116-125
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Rahil Jubrail,Pratt R. F.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00167a015

Reference72 articles.

1. The Determination of Ionization Constants

2. The amino acid sequence of Staphylococcus aureus penicillinase

3. Pre-steady state beta-lactamase kinetics. The trapping of a covalent intermediate and the interpretation of pH rate profiles.

4. Thermal denaturation of native and cross-linked bacillus cereus 569/II β-lactamase I

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