Literature summary for 3.4.22.60 extracted from

Miscione, G.P.; Calvaresi, M.; Bottoni, A.
Computational evidence for the catalytic mechanism of caspase-7. A DFT investigation (2010), J. Phys. Chem. B, 114, 4637-4645.

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Inhibitors

Inhibitors	Comment	Organism	Structure
Ac-DEVD-CHO	-	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-/-	catalytic mechanism of caspase-7 consisting of three distinct kinetic steps leading to the protonation of the catalytic His144 and the deprotonation of Cys186, which is activated as a nucleophile, DFT computational investigation using crystal structure with PDB code 1FIJ, the catalytic dyad is formed by His144 and Cys186, existence of an alternative reaction channel leading directly from the initial complex to the peptide bond cleavage in a single kinetic step, detailed overview. The reaction pathway is characterized by a high energy barrier	Homo sapiens	a

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Release 2023.1 (January 2023)