A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substrates
- 1 July 1977
- journal article
- research article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 114 (1), 119-132
- https://doi.org/10.1016/0022-2836(77)90286-8
Abstract
No abstract availableThis publication has 29 references indexed in Scilit:
- Studies on inhibitory effect of phosphoramidon and its analogs on thermolysinArchives of Biochemistry and Biophysics, 1975
- Modulation of Thermolysin Activity. Reversibility of Inactivation and SuperactivationIsrael Journal of Chemistry, 1974
- Relationship of the three dimensional structure of carboxypeptidase A to catalysisTetrahedron, 1974
- Evidence of an essential histidine residue in thermolysinBiochemistry, 1974
- Reversible inactivation and superactivation by covalent modification of thermolysinBiochemical and Biophysical Research Communications, 1973
- The structure of thermolysin: An electron density map at 2.3 Å resolutionJournal of Molecular Biology, 1972
- Carboxypeptidase A. Mechanistic analysisAccounts of Chemical Research, 1972
- Studies on the Bacillus subtilis neutral-protease- and Bacillus thermoproteolyticus thermolysin-catalyzed hydrolysis of dipeptide substratesBiochemistry, 1970
- The structure of carboxypeptidase A. VIII. Atomic interpretation at 0.2 nm resolution, a new study of the complex of glycyl-L-tyrosine with CPA, and mechanistic deductionsPhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1970
- Role of a Buried Acid Group in the Mechanism of Action of ChymotrypsinNature, 1969