Theoretical study of the CN bond breakage catalysed by the serine peptidases
- 1 February 1984
- journal article
- Published by Elsevier in Journal of Molecular Structure: THEOCHEM
- Vol. 107, 117-126
- https://doi.org/10.1016/0166-1280(84)80046-9
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- Unusually large electrostatic field effect of the buried aspartate in serine proteinases: Source of catalytic powerInternational Journal of Quantum Chemistry, 1983
- Role of local induced-fit of Ser 195 in β-trypsinFEBS Letters, 1982
- Theoretical calculations on proton-transfer energetics: studies of methanol, imidazole, formic acid, and methaneethiol as models for the serine and cysteine proteasesJournal of the American Chemical Society, 1981
- Neutron diffraction identifies His 57 as the catalytic base in trypsinNature, 1980
- Ab initio study of β-lactam antibiotics. I. Potential energy surface for the amidic CN bond breaking in the β-lactam + OH− reactionChemical Physics, 1980
- 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
- Molecular orbital studies of enzyme activity. 2. Nucleophilic attack on carbonyl systems with comments on orbital steeringJournal of the American Chemical Society, 1976
- Molecular orbital studies of enzyme activity: catalytic mechanism of serine proteinases.Proceedings of the National Academy of Sciences, 1976
- Molecular orbital studies of enzyme activity: I: Charge relay system and tetrahedral intermediate in acylation of serine proteinases.Proceedings of the National Academy of Sciences, 1975
- Role of a Buried Acid Group in the Mechanism of Action of ChymotrypsinNature, 1969