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Literature summary for 3.4.22.39 extracted from

  • Baniecki, M.L.; McGrath, W.J.; McWhirter, S.M.; Li, C.; Toledo, D.L.; Pellicena, P.; Barnard, D.L.; Thorn, K.S.; Mangel, W.F.
    Interaction of the human adenovirus proteinase with its 11-amino acid cofactor pVIc (2001), Biochemistry, 40, 12349-12356.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.39

Activating Compound

Activating Compound Comment Organism Structure
pVIc the enzyme requires two cofactors for maximal activity,the 11-amino acid residue peptide from the C-terminus of adenovirus precursor protein and the viral DNA. Influence of mutant pVIcs on Km-value and turnover number with (Leu-Arg-Gly-Gly-NH)2-rhodamine as substrate Human adenovirus sp.

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 influence of mutant pVIcs on Km-value with (Leu-Arg-Gly-Gly-NH)2-rhodamine as substrate Human adenovirus sp.

Organism

Organism UniProt Comment Textmining
Human adenovirus sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(Leu-Arg-Gly-Gly-NH)2-rhodamine + H2O
-
 Human adenovirus sp. ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information influence of mutant pVIcs on turnover number with (Leu-Arg-Gly-Gly-NH)2-rhodamine as substrate Human adenovirus sp.
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 influence of mutant pVIcs on turnover number with (Leu-Arg-Gly-Gly-NH)2-rhodamine as substrate Human adenovirus sp.