Literature summary for 3.4.21.4 extracted from

Ma, W.; Tang, C.; Lai, L.
Specificity of trypsin and chymotrypsin: loop-motion-controlled dynamic correlation as a determinant (2005), Biophys. J., 89, 1183-1193.

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Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P00760	-	-

Subunits

Subunits	Comment	Organism
More	study of dynamic properties of enzyme and chymotrypsin in Gaussion network model. Replacing the two loops of trypsin with those of chymotrypsin changes the motion style of trypsin into chymotrypsin-like, but not necessarily vice-versa. Cooperative motions of the two loops and the substrate-binding sites contribute to the activity and substrate specificity of trypsin and chymotrypsin	Bos taurus

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Release 2023.1 (January 2023)