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Literature summary for 2.7.10.2 extracted from

  • Adams Joseph, A.
    Activation loop phosphorylation and catalysis in protein kinases: is there functional evidence for the autoinhibitor model? (2003), Biochemistry, 42, 601-607.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
eukaryota

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + a protein eukaryota
-
ADP + a phosphoprotein
-
?

Organism

Organism UniProt Comment Textmining
eukaryota
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation regulates the enzyme activity, the enzyme is phosphorylated at the activation loop eukaryota

Reaction

Reaction Comment Organism Reaction ID
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate regulation of enzyme activity involves the activation loop, a polypeptide region outside the active site cleft, which is reversibly phosphorylated eukaryota

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + a protein
-
eukaryota ADP + a phosphoprotein
-
?

Synonyms

Synonyms Comment Organism
nonreceptor PTK
-
eukaryota
v-Fps
-
eukaryota

Cofactor

Cofactor Comment Organism Structure
ATP the binding site is a deep pocket lined by hydrophobic residues, enzyme affinity of v-Fps for ATP is not influenced by phosphorylation of the activation loop eukaryota