Structural analysis of the inhibition of thermolysin by an active-site-directed irreversible inhibitor
- 4 January 1983
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 22 (1) , 236-240
- https://doi.org/10.1021/bi00270a034
Abstract
Note: In lieu of an abstract, this is the article's first page.Keywords
This publication has 20 references indexed in Scilit:
- Inhibition of thermolysin and carboxypeptidase A by phosphoramidatesBiochemistry, 1979
- Binding of the biproduct analog L-benzylsuccinic acid to thermolysin determined by X-ray crystallography.Journal of Biological Chemistry, 1979
- Catalytic role of the metal ion of carboxypeptidase A in ester hydrolysis.Journal of Biological Chemistry, 1979
- Active site directed irreversible inhibition of thermolysinBiochemistry, 1978
- Peptide hydroxamic acids as inhibitors of thermolysinBiochemistry, 1978
- Comparison of the structures of carboxypeptidase A and thermolysin.Journal of Biological Chemistry, 1977
- A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substratesJournal of Molecular Biology, 1977
- Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for the mechanism of catalysisBiochemistry, 1977
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- Unified picture of mechanisms of catalysis by carboxypeptidase A.Proceedings of the National Academy of Sciences, 1977