Literature summary for 3.4.24.86 extracted from

Liu, S.; Liu, S.; Wang, Y.; Liao, Z.
The P2/P2 sites affect the substrate cleavage of TNF-alpha converting enzyme (TACE) (2014), Mol. Immunol., 62, 122-128.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
docking of nine-residue peptide PLAQA-VRSS from proTNF-alpha. The peptide adopts an anti-parallel beta-sheet conformation against a nearby beta-sheet of the protein. In the complexmodel, the side-chains of residues P2 and P2' are largely exposed,and do not form highly favorable interactions	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P78536	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	mutations at the P2 site and the P2' site of the substrate peptide largely affect the peptide cleavage efficiency in the enzymaticassay. The P2/P2'sites may affect the efficiency of the conformation search for the correct peptide orientation, which in turn affects the substrate cleavage efficiency. Peptide PRYEA?YKMG is not a substrate	Homo sapiens	?	-	?
PLAAAVFSS + H2O	mutant peptide derived from TNF-alpha, very poor substrate	Homo sapiens	PLAAA + VFSS	-	?
PLAMAVMSS + H2O	mutant peptide derived from TNF-alpha, very poor substrate	Homo sapiens	PLAMA + VMSS	-	?
PLAQAVRSS + H2O	peptide derived from TNF-alpha	Homo sapiens	PLAQA + VRSS	-	?

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Release 2023.1 (January 2023)