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Literature summary for 3.4.21.97 extracted from

  • Khayat, R.; Batra, R.; Qian, C.; Halmos, T.; Bailey, M.; Tong, L.
    Structural and biochemical studies of inhibitor binding to human cytomegalovirus protease (2003), Biochemistry, 42, 885-891.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor diffusion method, crystal structure of the wild-typelike mutant enzyme A143Q in complex with peptidomimetic inhibitors, crystal structure of peptidomimetic inhibitor in complex with the E31R mutant enzyme Human betaherpesvirus 5

Protein Variants

Protein Variants Comment Organism
A143Q/E31R the ratio of turnover number to Km-value is 44.6fold lower than that for the wild-typelike mutant A143Q Human betaherpesvirus 5
A143Q/E31S the ratio of turnover number to Km-value is 4.8fold lower than that for the wild-typelike mutant A143Q Human betaherpesvirus 5
A143Q/R137E the ratio of turnover number to Km-value is 6.3fold lower than that for the wild-typelike mutant A143Q Human betaherpesvirus 5

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
Human betaherpesvirus 5

Organism

Organism UniProt Comment Textmining
Human betaherpesvirus 5
-
-
-

Synonyms

Synonyms Comment Organism
human cytomegalovirus protease
-
Human betaherpesvirus 5

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information
-
Human betaherpesvirus 5
additional information
-
2-[5-Amino-2-(4-fluoro-phenyl)-6-oxo-6H-pyrimidin-1-yl]-N-(1-benzyl-2-oxo-2-thiazol-2-yl-ethyl)-acetamide
-
Human betaherpesvirus 5