Literature summary for 3.4.21.1 extracted from

Wang, J.; Zheng, X.; Wang, W.; Guo, H.; Liu, R.; Zong, W.
A study on the interaction between cadmium and alpha-chymotrypsin and the underlying mechanisms (2019), J. Biochem. Mol. Toxicol., 33, e22248 .

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Cd2+	CdCl2 binds to the enzyme mainly via electrostatic forces with binding sites, leading to the increase of alpha-helix and the decrease of beta-sheet. The interaction between CdCl2 and alpha-ChT loosens the protein skeleton and increases the molecular volume of the enzyme. CdCl2 first binds to the interface of the enzyme and then interacts with the key residues His57 or Asp102 or both in the active sites, leading to the activity inhibition of the enzyme under the exposure of high CdCl2 concentrations	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P00766	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
pancreas	-	Bos taurus	-

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Release 2023.1 (January 2023)