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Catalytic Site Atlas Version 2.2.12
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CSA entry for 1jag
Original Entry
Title:
Transferase
Compound:
Deoxyguanosine kinase
Mutant:
No
UniProt/Swiss-Prot:
Q16854-DGK_HUMAN
EC Class:
2.7.1.113
Other CSA Entries:
Overview of all sites for 1jag
Homologues of 1jag
Entries for UniProt/Swiss-Prot: Q16854
Entries for EC: 2.7.1.113
Other Databases:
PDB entry: 1jag
PDBsum entry: 1jag
UniProt/Swiss-Prot: Q16854
IntEnz entry: 2.7.1.113
Literature Report:
Introduction:
Deoxyribonucleoside kinases such as deoxyguanoside kinase phosphorylate deoxyribonucleosides. The human form is highly specific for purine substrates. Deoxynucleoside kinases are key in chemotherapy of cancer as they are needed to activate nucleoside analogues by phosphorylation. dGK is involved in the regulation of dGTP and dATP pools, and may possibly have a role in apoptosis.
Mechanism:
Activation of the 5'-OH of the deoxyribose by deprotonation with Glu 70 allows a nucleophilic attack of the gamma-phosphate of the phosphate donor. The deprotonation is facilitated by Arg 142.
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Found by:
Literature reference 

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
GLUA 70 0Sidechain
Acid/baseSubstrate
Base in deprotonation of 5' hydroxy group of nucleoside.
Evidence from paper Evidence concerns Evidence type
PubMed ID 12363036 Current protein Structural similarity to homologue of known mechanism
PubMed ID 14623087 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 12363036 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 15896737 Current protein Conservation of residue

ResidueChainNumberUniProt numberFunctional part FunctionTargetDescription
ARGA 142 0Sidechain
ElectrostaticResidue
Facilitates deprotonation by Glu 70.
Evidence from paper Evidence concerns Evidence type
PubMed ID 14623087 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 15896737 Current protein Conservation of residue
PubMed ID 12363036 Current protein Residue is positioned appropriately (ligand position known)
PubMed ID 12363036 Current protein Structural similarity to homologue of known mechanism
References:
1
Deoxyribonucleoside kinases: two enzyme families catalyze the same reaction.
M. P. Sandrini and J. Piskur
Trends Biochem Sci 30, (5) 225-8, (2005).
15896737
2
Structure and function of cellular deoxyribonucleoside kinases.
S. Eriksson and B. Munch-Petersen and K. Johansson and H. Eklund
Cell Mol Life Sci 59, (8) 1327-46, (2002).
12363036
3
Mitochondrial deoxyguanosine kinase mutations and mitochondrial DNA depletion syndrome.
L. Wang and S. Eriksson
FEBS Lett 554, (3) 319-22, (2003).
14623087
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