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Subtilisin

Known as: Subtilisin [Chemical/Ingredient] 
A serine endopeptidase isolated from Bacillus subtilis. It hydrolyzes proteins with broad specificity for peptide bonds, and a preference for a large… 
National Institutes of Health

Related topics

Related topics

9 relations
In BloodProcess of secretionantagonists & inhibitorsaspects of radiation effects

Broader (2)

Serine ProteasesSubtilisins

Papers overview

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Review
2005
Review
2005
Tip of another iceberg: Drosophila serpins.
Highly Cited
1997
Highly Cited
1997
Can conformational changes be responsible for solvent and excipient effects on the catalytic behavior of subtilisin Carlsberg in organic solvents?
We developed an FTIR (Fourier transform infrared) methodology for quantitatively assessing the secondary structure of proteins… 
Highly Cited
1993
Highly Cited
1993
Interaction of the tail domain of high molecular weight subunits of neurofilaments with the COOH-terminal region of tubulin and its regulation by tau protein kinase II.
Highly Cited
1993
Highly Cited
1993
Structure and function of eukaryotic proprotein processing enzymes of the subtilisin family of serine proteases.
Production of a broad spectrum of regulatory proteins in eukaryotes occurs via an intricate cascade of biosynthetic and secretory… 
Highly Cited
1990
Highly Cited
1990
Structure and expression of mouse furin, a yeast Kex2-related protease. Lack of processing of coexpressed prorenin in GH4C1 cells.
Highly Cited
1988
Highly Cited
1988
The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case.
A weak Ca2+ binding site in the bacterial serine protease subtilisin BPN' (EC 3.4.21.14) was chosen as a model to explore the… 
Highly Cited
1988
Highly Cited
1988
Structure and stability of thermophilic enzymes. Studies on thermolysin.
Review
1981
Review
1981
Domain structure of bacteriophage fd adsorption protein
Highly Cited
1974
Highly Cited
1974
Studies on the amphipathic nature of the membrane proteins in Semliki Forest virus.
Highly Cited
1968
Highly Cited
1968
Isolation and amino acid sequence of caerulein, the active decapeptide of the skin of hyla caerulea.
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