Specificity of α-chymotrypsin. Dipeptide substrates

Specificity of chymotrypsin B.

Brown, Shupe, and Laskowski (1) have described the isolation, from beef pancreas, of a crystalline proteolytic enzyme which they have named “activated protein B” or “chymotrypsin B.” Through the kindness of Dr. Laskowski who provided us with a 4 times recrystallized sample of this enzyme, it was possible to examine its action on a series of synthetic peptides and peptide derivatives. The data p...

Facile synthesis of bis(indolyl)methanes catalyzed by α-chymotrypsin.

A mild and efficient method catalyzed by α-chymotrypsin was developed for the synthesis of bis(indolyl)methanes through a cascade process between indole and aromatic aldehydes. In the ethanol aqueous solution, a green medium, a wide range of aromatic aldehydes could react with indole to afford the desired products with moderate to good yields (from 68% to 95%) using a little α-chymotrypsin as c...

Α-glucosidase and Chymotrypsin Inhibiting Lignans from Commiphora Mukul

Phytochemical investigation of the whole plant of Commiphora mukul Engl. resulted in the isolation of two lignans, epiexcelsin (1) and 5′-demethoxyepiexcelsin (2) which are reported for the first time from this species. The structure elucidation of the isolated compounds was based on 1D and 2DNMR analysis and by the comparison with the published data. The lignans 1 and 2 showed significant inhi...

The Specificity of Enzymes for Certain Substrates

Comparative studies of the specificities of -chymotrypsin and subtilisin BPN'. Studies with flexible and 'locked' substrates.

Subtilisin BPN' hydrolysed N-acetyl-l-3-(2-naphthyl)-alanine methyl ester, N-acetyl-l-leucine methyl ester and N-acetyl-l-valine methyl ester, faster than alpha-chymotrypsin. Of eight ;locked' substrates tested, only methyl 5,6-benzindan-2-carboxylate was hydrolysed faster by subtilisin, whereas the other esters were better substrates for chymotrypsin. Compared with the values for chymotrypsin,...