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Literature summary for 2.7.11.1 extracted from

  • Niefind, K.; Pütter, M.; Guerra, B.; Issinger, O.G.; Schomburg, D.
    GTP plus water mimic ATP in the active site of protein kinase CK2 (1999), Nat. Struct. Biol., 6, 1100-1103.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Zea mays

Crystallization (Commentary)

Crystallization (Comment) Organism
the structures of the catalytic subunit of protein kinase CK2 from Zea mays complexed with Mg2+ and with analogs of ATP or GTP are determined to 2.2 A resolution Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays P28523
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Zea mays

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + a protein the enzyme shows dual-cosubstrate specificity because it provides enough space for a hydrogenbonding frame-shift at the nucleotide-binding site and because water molecules allow the purine bases to use the full hydrogen-bonding potential of this site Zea mays ADP + a phosphoprotein
-
?
GTP + a protein the enzyme shows dual-cosubstrate specificity because it provides enough space for a hydrogenbonding frame-shift at the nucleotide-binding site and because water molecules allow the purine bases to use the full hydrogen-bonding potential of this site Zea mays GDP + a phosphoprotein
-
?

Subunits

Subunits Comment Organism
heterotetramer
-
Zea mays

Synonyms

Synonyms Comment Organism
protein kinase CK2
-
Zea mays