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Literature summary for 2.7.10.1 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
Search for more literature for 2.7.10.1

Activating Compound

Activating Compound Comment Organism Structure
additional information activation mechanism eukaryota

Crystallization (Commentary)

Crystallization (Comment) Organism
X-ray diffraction structure analysis of InRK and of FGFR with phosphorylated activation loop embedded in the substrate pocket eukaryota

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information InRK: random kinetic mechanism, reaction kinetic can be influenced by the sort of substrate eukaryota

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 eukaryota 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cd2+ can partially substitue Mg2+ eukaryota
Co2+ can partially substitue Mg2+ eukaryota
Mg2+
-
 eukaryota
Mg2+ dependent on, Mg2+ is the physiologic metal ion, other divalent cations are able to support nucleotide binding, but only Mn2+, Co2+, and Cd2+ can substitute Mg2+ in supporting the catalytic activity eukaryota
Mn2+ can partially substitue 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
-
 ?
additional information eukaryota mutations in the glycine-riche loop of MET can cause papillary renal-cell carcinomas ?
-
 ?

Organism

Organism UniProt Comment Textmining
eukaryota
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein phosphorylation regulates the enzyme activity, but has only a small influence on substrate binding by InRK, and no influence on substrate binding of Tie-2 eukaryota

Reaction

Reaction Comment Organism Reaction ID
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate reaction mechanism eukaryota
a
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
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + a protein
-
 eukaryota ADP + a phosphoprotein
-
 ?
additional information mutations in the glycine-riche loop of MET can cause papillary renal-cell carcinomas eukaryota ?
-
 ?
additional information poor activity on free amino acids, consensus sequence of InRK is YM-MM, and of EGFR E-EEYF eukaryota ?
-
 ?

Synonyms

Synonyms Comment Organism
Egfr
-
 eukaryota
epidermal growth factor receptor
-
 eukaryota
FGFR
-
 eukaryota
fibroblast growth factor receptor
-
 eukaryota
InRK
-
 eukaryota
insulin receptor kinase
-
 eukaryota
MET
-
 eukaryota
receptor PTK
-
 eukaryota
Tie-2
-
 eukaryota
tyrosine kinase domain of the insulin receptor
-
 eukaryota

Cofactor

Cofactor Comment Organism Structure
ATP dependent on eukaryota
ATP the binding site is a deep pocket lined by hydrophobic residues, enzyme affinity of Tie-2 for ATP is not influenced by phosphorylation of the activation loop eukaryota