Protein Variants | Comment | Organism |
---|---|---|
S132A | mutant enzyme is catalytically inactive | Human betaherpesvirus 5 |
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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Human betaherpesvirus 5 | - |
- |
- |
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 | 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 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 |