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Subtilisins

Known as: Subtilisins [Chemical/Ingredient] 
A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.-
National Institutes of Health

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Narrower (38)

AprS protein, BacillusAquifex pyrophilus serine-type proteaseBacillus amyloliquefaciens Serine ProteaseDurazym
In BloodProcess of secretionantagonists & inhibitorsaspects of radiation effects

Broader (1)

Serine Endopeptidases

Papers overview

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2009
2009
Photoreactivity of histidyl residues in subtilisins Novo and DY. Photooxidation of subtilisins.
Subtilisins Novo and DY were photoinactivated in the presence of methylene blue according to first order kinetics. The… 
2009
2009
Modification of arginine residues in subtilisins Novo and Carlsberg. Effect on the protein structure and enzymatic activity.
The modification of arginine 186 and arginine 247 in subtilisin Novo as well as the four guanidino groups in subtilisin Carlsberg… 
1990
1990
[Crystal structure of thermitase and stability of subtilisins].
Crystal structure of thermitase, a serine proteinase from Thermoactinomyces vulgaris, has been determined by X-ray diffraction at… 
1986
1986
Fluorescence technique for comparative studies of substrate-binding subsites in serine proteinases. Application to subtilisins.
A fluorescence technique for comparative studies of substrate-binding subsites in serine proteinases is described. It consists of… 
1983
1983
Intramolecular distances between tryptophan residues and the active-site serine residue in alkaline bacterial proteinases as measured by fluorescence energy-transfer studies.
Singlet-singlet energy transfer from the tryptophan residues to an active-site-serine-bound 5-dimethylaminonaphthalene-1… 
1981
1981
[Extracellular serine proteinase of Bacillus thuringiensis].
Pure extracellular serine proteinase has been isolated from a broth filtrate of Bacillus thuringiensis, strain 69-6R by… 
1979
1979
Interactions of BPN' and Carlsberg subtilisins with peptides containing aromatic amino acids at the C-terminus. Specific rate enhancement due to the secondary enzyme-substrate interaction.
The interaction between BPN' or Carlsberg subtilisins and peptides of the type Ac-Glyn-X-OMe (n = 0, 1, 2, 3), where X denotes… 
1979
1979
Conformation of the active site of thiolsubtilisin: reaction with specific chloromethyl ketones and arylacryloylimidazoles.
The conformation of the active site of thiolsubtilisin, prepared from subtilisin by transformation of the active site Ser to Cys… 
1978
1978
Kinetic specificities of BPN' and Carlsberg subtilisins. Mapping the aromatic binding site.
The kinetic specificities of BPN' and Carlsberg subtilisins [EC 3.4.21.14] were examined with various nucleus-substituted… 
1968
1968
The degradation of the B-chain of oxidized insulin by two subtilisins and their succinylated and N-carbamylated derivatives.