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Literature summary for 2.7.10.2 extracted from

  • Weijland, A.; Neubauer, G.; Courtneidge, S.A.; Mann, M.; Wierenga, R.K.; Superti-Furga, G.
    The purification and characterization of the catalytic domain of Src expressed in Schizosaccharomyces pombe. Comparison of unphosphorylated and tyrosine phosphorylated species (1996), Eur. J. Biochem., 240, 756-764.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
catalytic domain Src including the C-terminal tail Src-CD, expressed in Schizosaccharomyces pombe Gallus gallus

Inhibitors

Inhibitors Comment Organism Structure
additional information completely inhibited by an excess of substrate peptide Gallus gallus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information the overall activity kcat of the catalytic domain Src, Src-CD, including the C-terminal tail for two exogenous substrates, the Src substrate peptide AEEEIYGEFEAKKKK and denatured enolase is about 10 times higher than that of wild-type Src. The kcat values for phosphorylation of the Src substrate peptide are similar for the unphosphorylated and monophosphorylated Src-CD, 50 min-1, but the apparent Km values differ significantly, approximately 0.003 mM and 0.010 mM, respectively Gallus gallus

Organism

Organism UniProt Comment Textmining
Gallus gallus P00523
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification protein expressed in Schizosaccharomyces pombe is a mixture of unphosphorylated, 80%, and mono-phosphorylated, 20%, species. The mono-phosphorylated form is phosphorylated either at Tyr416 or at Tyr436 Gallus gallus

Purification (Commentary)

Purification (Comment) Organism
catalytic domain Src including the C-terminal tail Src-CD, expressed in Schizosaccharomyces pombe Gallus gallus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
AEEEIYGEFEAKKKK + ATP
-
Gallus gallus ? + ADP
-
?
denatured enolase + ATP
-
Gallus gallus phosphorylated denatured enolase + ADP
-
?
additional information catalytic domain Src including the C-terminal tail autophosphorylates and efficiently phosphorylates substrate peptides and proteins. Autophosphorylation occurs by an intermolecular mechanism Gallus gallus ?
-
?

Synonyms

Synonyms Comment Organism
proto-oncogene tyrosine-protein kinase SRC
-
Gallus gallus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information the overall activity kcat of the catalytic domain Src, Src-CD, including the C-terminal tail for two exogenous substrates, the Src substrate peptide AEEEIYGEFEAKKKK and denatured enolase is about 10 times higher than that of wild-type Src. The kcat values for phosphorylation of the Src substrate peptide are similar for the unphosphorylated and monophosphorylated Src-CD, 50 min-1 Gallus gallus