Literature summary for 3.4.22.15 extracted from

Hood, C.L.; Abraham, J.; Boyington, J.C.; Leung, K.; Kwong, P.D.; Nabel, G.J.
Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity (2010), J. Virol., 84, 2972-2982.

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Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
Zaire Ebola virus glycoprotein + H2O	Homo sapiens	-	?	three cleavage fragments with masses of 23000, 19000, and 4000 Da. Cleavage removes a glycosylated glycan cap and mucin-like domain (MUC domain) and exposes the conserved core residues implicated in receptor binding	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
Zaire Ebola virus glycoprotein + H2O	-	Homo sapiens	?	three cleavage fragments with masses of 23000, 19000, and 4000 Da. Cleavage removes a glycosylated glycan cap and mucin-like domain (MUC domain) and exposes the conserved core residues implicated in receptor binding	?

Synonyms

Synonyms	Comment	Organism
CatL	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	CatL cleavage of Zaire Ebola virus glycoprotein exposes its receptor-binding domain, thereby facilitating access to a putative cellular receptor in steps that lead to membrane fusion	Homo sapiens

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Release 2023.1 (January 2023)