Comparison of the structures of carboxypeptidase A and thermolysin.
Open Access
- 1 November 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (21) , 7704-7710
- https://doi.org/10.1016/s0021-9258(17)41025-8
Abstract
No abstract availableThis publication has 30 references indexed in Scilit:
- 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
- A method of obtaining a stereochemically acceptable protein model which fits a set of atomic coordinatesActa Crystallographica Section A, 1976
- Environment and conformation dependent sensitivity of the arsanilazotyrosine-248 carboxypeptidase A chromophoreBiochemistry, 1975
- Interactions of histidine and other imidazole derivatives with transition metal ions in chemical and biological systemsChemical Reviews, 1974
- The structure of thermolysin: An electron density map at 2.3 Å resolutionJournal of Molecular Biology, 1972
- X-ray crystallographic study of the binding of peptide chloromethyl ketone inhibitors to subtilisin BPNBiochemistry, 1972
- The Atomic Structure of Erythrocruorin in the Light of the Chemical Sequence and its Comparison with MyoglobinEuropean Journal of Biochemistry, 1971
- A hydrogen-bond network at the active site of subtilisin BPN'Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1970
- Relation between γ- and α-chymotrypsinJournal of Molecular Biology, 1968