Literature summary for 3.4.21.97 extracted from

Chen, P.; Tsuge, H.; Almassy, R.J.; Gribskov, C.L.; Katoh, S.; Vanderpool, D.L.; Margosiak, S.A.; Pinko, C.; Matthews, D.A.; Kan, C.C.
Structure of the human cytomegalovirus protease catalytic domain reveals a novel serine protease fold and catalytic triad (1996), Cell, 86, 835-843.

Search for more literature for 3.4.21.97

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Human betaherpesvirus 5

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the catalytic domain at 2.5 A resolution	Human betaherpesvirus 5

Organism

Organism	UniProt	Comment	Textmining
Human betaherpesvirus 5	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
cytomegalovirus assembly protein precursor + H2O	cleavage at the C-terminal maturation site, i.e. M-site, between Ala643-Ser644, autoproteolytic cleavage at the R-site between Ala256-Ser257, internal cleavage sites, i.e. I-sites are Ala143-Ala144, Ala209-Ser210, cleavage occurs at the M-site first, followed by the R-site and then the I-sites	Human betaherpesvirus 5	?	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)