On the role of peripheral interactions in specificity of chymosin.
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.
Safro
M G
MG
Institute of Molecular Biology, Academy of Sciences of the USSR, Moscow.
Andreeva
N S
NS
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D012085:Chymosin / Q000378:metabolism; D004563:Electrochemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D013379:Substrate Specificity / Q000502:physiology
D012085:Chymosin