On the role of peripheral interactions in specificity of chymosin

Safro, M.G.; Andreeva, N.S.

Biochemistry International 20(3): 555-561

1990


ISSN/ISBN: 0158-5231
PMID: 2111997
Document Number: 357111
Chymosin is distinguished by a high level of milk-clotting activity which is the consequence of the specific cleavage of the Phe (105)-Met (106) bond of .kappa.-casein. Based on modelling considerations it was proposed that milk-clotting activity of chymosin is associated with electrostatic interactions of a charged segment His-Pro-His-Pro-His (98-102) of casein and the outer loop of the enzyme containing Glu-244, Asp-246 and Asp-248.

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