Structures of product and inhibitor complexes of Streptomyces griseus protease A at 1.8 Å resolution: A model for serine protease catalysis
- 25 November 1980
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 144 (1), 43-88
- https://doi.org/10.1016/0022-2836(80)90214-4
Abstract
No abstract availableKeywords
This publication has 78 references indexed in Scilit:
- Crystallographic studies of the dynamic properties of lysozymeNature, 1979
- Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of .alpha.-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteasesJournal of the American Chemical Society, 1978
- Active centers of Streptomyces griseus protease 1, Streptomyces griseus protease 3, and α-chymotrypsin: enzyme-substrate interactionsBiochemistry, 1978
- Molecular Orbital studies on the Enzymatic Reaction Mechanism of Serine Proteases. I. Charge Relay System in Substrate Free StateJournal of the Physics Society Japan, 1977
- Crystal structure of elastase–substrate complex at −55 °CNature, 1976
- The active centers of Streptomyces griseus protease 3 and α-chymotrypsin: enzyme-substrate interactions remote from the scissile bondBiochemistry, 1976
- The active centers of Streptomyces griseus protease 3, α-chymotrypsin, and elastase: enzyme-substrate interactions close to the scissile bondBiochemistry, 1976
- ChymotrypsinCRC Critical Reviews in Biochemistry, 1973
- Studies of the Heterogeneity of Streptomyces griseus Protease. Isolation and Characterization of an Alkaline Serine Protease from Commercial Pronase-P Derived from Streptomyces griseus Kl.Acta Chemica Scandinavica, 1973
- The Mechanism of α-Chymotrypsin-catalyzed Hydrolyses1-3Journal of the American Chemical Society, 1962