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Literature summary for 2.7.10.2 extracted from

  • Lin, X.; Ayrapetov, M.K.; Lee, S.; Parang, K.; Sun, G.
    Probing the communication between the regulatory and catalytic domains of a protein tyrosine kinase, Csk (2005), Biochemistry, 44, 1561-1567.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
AMpYSSV CBP-based phosphopeptide, activates Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant GST-fusion Csk proteins Homo sapiens

Protein Variants

Protein Variants Comment Organism
K361G/K362A the mutant shows reduced phosphorylation activity compared to the wild-type enzyme, especially with substrate poly(Glu4-Tyr) Homo sapiens
additional information construction of mutants DSH3 and DSH2 lacking the SH3 and SH2 domains, respectively, the mutants show decreased binding to phosphorylation sites of substrates compared to the wild-type enzyme, mutant DSH2 also shows reduced phosphorylation activity Homo sapiens
R389A the mutant shows reduced phosphorylation activity compared to the wild-type enzyme, especially with substrate [kdSrc kinase]-L-tyrosine Homo sapiens
W188A the mutant shows increased binding to phosphorylation sites of substrates but reduced phosphorylation activity compared to the wild-type enzyme, especially with substrate poly(Glu4-Tyr) Homo sapiens
W188F the mutant shows increased binding to phosphorylation sites of substrates but reduced phosphorylation activity compared to the wild-type enzyme, especially with substrate poly(Glu4-Tyr) Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.015
-
[kdSrc kinase]-L-tyrosine pH 8.0, 30°C, recombinant wild-type Csk Homo sapiens
0.017
-
[kdSrc kinase]-L-tyrosine pH 8.0, 30°C, recombinant W188F Csk mutant Homo sapiens
0.027
-
[kdSrc kinase]-L-tyrosine pH 8.0, 30°C, recombinant DSH3 Csk mutant Homo sapiens
0.032
-
[kdSrc kinase]-L-tyrosine pH 8.0, 30°C, recombinant K361G/K362A Csk mutant Homo sapiens
0.042
-
[kdSrc kinase]-L-tyrosine pH 8.0, 30°C, recombinant DSH2 Csk mutant Homo sapiens
0.068
-
[kdSrc kinase]-L-tyrosine pH 8.0, 30°C, recombinant W188A Csk mutant Homo sapiens
0.15
-
poly(Glu4-Tyr) pH 8.0, 30°C, recombinant wild-type Csk Homo sapiens
0.164
-
poly(Glu4-Tyr) pH 8.0, 30°C, recombinant DSH2 Csk mutant Homo sapiens
0.204
-
poly(Glu4-Tyr) pH 8.0, 30°C, recombinant W188A Csk mutant Homo sapiens
0.299
-
poly(Glu4-Tyr) pH 8.0, 30°C, recombinant W188F Csk mutant Homo sapiens
0.328
-
poly(Glu4-Tyr) pH 8.0, 30°C, recombinant DSH3 Csk mutant Homo sapiens
0.659
-
poly(Glu4-Tyr) pH 8.0, 30°C, recombinant K361G/K362A Csk mutant Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant GST-fusion Csk proteins by glutathione affinity chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + poly(Glu4-Tyr)
-
Homo sapiens ADP + poly(Glu4-Tyr)-L-tyrosine phosphate
-
?
ATP + [kdSrc kinase]-L-tyrosine i.e. kinase-defective chicken Src mutant K295M Homo sapiens ADP + [kdSrc kinase]-L-tyrosine phosphate
-
?
additional information Csk-substrate interaction requires the SH2 and SH3 enzyme domains Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
More Csk structure analysis, PDB code 1K9A, compared to tyrosine kinase Hsk, PDB code 1QCF Homo sapiens

Synonyms

Synonyms Comment Organism
Csk
-
Homo sapiens
Protein tyrosine kinase
-
Homo sapiens
PTK
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information
-
Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP binding lobe structure Homo sapiens