The conversion of serine at the active site of subtilisin to cysteine: a "chemical mutation".
- 1 November 1966
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 56 (5), 1606-1611
- https://doi.org/10.1073/pnas.56.5.1606
Abstract
The hydroxyl of the serine in the active center of subtilisin has been converted to a sulfhydryl group. The resulting enzyme, thiol-sub-tillsin, is at most 1/100 as active as native subtilisin toward normal ester and peptlde substrates. Since model experiments indicated that the thiol group should in general be more reactive than a hydroxyl group, the loss of activity of thiol-subtUisln indicates the enormous sensitivity of catalytic residues to subtle changes in structure.This publication has 14 references indexed in Scilit:
- The Formation of Anhydrochymotrypsin by Removing the Elements of Water from the Serine at the Active Site1Journal of the American Chemical Society, 1966
- A Change in Specificity of Chymotrypsin Caused by Chemical Modification of Methionine ResiduesJournal of Biological Chemistry, 1966
- Cytochrome cAdvances in protein chemistry, 1966
- Studies on the Mechanism and Active Site for the Esterolytic Activity of 3-Phosphoglyceraldehyde DehydrogenaseJournal of Biological Chemistry, 1964
- A Kinetic Study of the Reaction of Thiols with p-Nitrophenyl Acetale*Biochemistry, 1964
- ROLE OF SERINE IN CHYMOTRYPSIN ACTION. CONVERSION OF THE ACTIVE SERINE TO DEHYDROALANINEProceedings of the National Academy of Sciences, 1963
- The Effect of Substituents on the Deacylation of Benzoyl-ChymotrypsinsBiochemistry, 1962
- Amino-acid Sequence about the Reactive Serine of a Proteolytic Enzyme from Bacillus subtilisNature, 1960
- A COMPARISON OF 2 PROTEINASES FROM BACILLUS-SUBTILIS1960
- IMIDAZOLE CATALYSIS .3. GENERAL BASE CATALYSIS AND THE REACTIONS OF ACETYL IMIDAZOLE WITH THIOLS AND AMINES1959