Proton nuclear magnetic resonance evidence for the absence of a stable hydrogen bond between the active site aspartate and histidine residues of native subtilisins and for its presence in thiolsubtilisins
- 1 October 1981
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 20 (22) , 6366-6370
- https://doi.org/10.1021/bi00525a013
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 6 references indexed in Scilit:
- Neutron diffraction identifies His 57 as the catalytic base in trypsinNature, 1980
- (Diisopropylphosphoryl)serine proteinases. Proton and phosphorus-31 nuclear magnetic resonance-pH titration studiesBiochemistry, 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
- Hydrogen bonds in serine proteinases and their complexes with protein proteinase inhibitors. Proton nuclear magnetic resonance studiesBiochemistry, 1978
- Re-examination of the charge relay system in subtilisin comparison with other serine proteases.Journal of Biological Chemistry, 1977
- The conversion of serine at the active site of subtilisin to cysteine: a "chemical mutation".Proceedings of the National Academy of Sciences, 1966