EC Number |
Title |
Organism |
---|
3.4.21.81 | Active centers of alpha-chymotrypsin and of Streptomyces griseus proteases 1 and 3. S2-P2 enzyme-substrate interactions |
Streptomyces griseus |
3.4.21.81 | Active-site variants of Streptomyces griseus protease B with peptide-ligation activity |
Streptomyces griseus |
3.4.21.81 | Additivity-based design of the strongest possible turkey ovomucoid third domain inhibitors for porcine pancreatic elastase (PPE) and Streptomyces griseus protease B (SGPB) |
Streptomyces griseus |
3.4.21.81 | Amino acid sequence of Streptomyces griseus protease B, A MAJOR COMPONENT OF Pronase |
Streptomyces griseus |
3.4.21.81 | Characterization and structure of genes for proteases A and B from Streptomyces griseus |
Streptomyces griseus |
3.4.21.81 | Cleavage of peptide bonds bearing ionizable amino acids at P(1) by serine proteases with hydrophobic S(1) pocket |
Streptomyces griseus |
3.4.21.81 | Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases |
Streptomyces griseus |
3.4.21.81 | Contribution of peptide bonds to inhibitor-protease binding: crystal structures of the turkey ovomucoid third domain backbone variants OMTKY3-Pro18I and OMTKY3-psi[COO]-Leu18I in complex with Streptomyces griseus proteinase B (SGPB) and the structure of the free inhibitor, OMTKY-3-psi[CH2NH2+]-Asp19I |
Streptomyces griseus |
3.4.21.81 | Crystal structure studies and inhibition kinetics of tripeptide chloromethyl ketone inhibitors with Streptomyces griseus protease B |
Streptomyces griseus |
3.4.21.81 | Determination of the cleavage specificity of Streptomyces griseus protease B in the presence of guanidinium chloride |
Streptomyces griseus |