Literature summary for 3.4.21.97 extracted from

Khayat, R.; Batra, R.; Bebernitz, G.A.; Olson, M.W.; Tong, L.
Characterization of the monomer-dimer equilibrium of human cytomegalovirus protease by kinetic methods (2004), Biochemistry, 43, 316-322.

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Protein Variants

Protein Variants	Comment	Organism
S132A	mutant enzyme is catalytically inactive	Human betaherpesvirus 5

General Stability

General Stability	Organism
dimers of the enzyme are stabilized in high-salt buffer. The Kd for the dimer decreases by 260fold, from 0.008 mM to 31 nM, going from the low-salt to the high-salt buffer	Human betaherpesvirus 5

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0118	0.0196	acetyl-Cys-tert-butylglycine-tert-butylglycine-Asn(Me)2-Ala-7-amido-4-methylcoumarin	24°C	Human betaherpesvirus 5

Organism

Organism	UniProt	Comment	Textmining
Human betaherpesvirus 5	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala-Ser-Ser-Arg-Leu-Ala((2'-aminoethyl)amino-naphthalene-1)sulfonic acid + H2O	-	Human betaherpesvirus 5	4-(4'-dimethylaminophenylazo)benzoyl-Arg-Gly-Val-Val-Asn-Ala + Ser-Ser-Arg-Leu-Ala((2'-aminoethyl)amino-naphthalene-1)sulfonic acid	-	?
acetyl-Cys-tert-butylglycine-tert-butylglycine-Asn(Me)2-Ala-7-amido-4-methylcoumarin + H2O	-	Human betaherpesvirus 5	acetyl-Cys-tert-butylglycine-tert-butylglycine-Asn(Me)2-Ala + 7-amino-4-methylcoumarin	-	?

Subunits

Subunits	Comment	Organism
dimer	the enzyme exists in a monomer/dimer equilibrium in solution, but only the dimer form is catalytically active. The stability of the dimer is affected by the presence of anti-chaotrophic agents	Human betaherpesvirus 5

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.1	0.16	acetyl-Cys-tert-butylglycine-tert-butylglycine-Asn(Me)2-Ala-7-amido-4-methylcoumarin	24°C	Human betaherpesvirus 5

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Release 2023.1 (January 2023)