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- Name help_outline a 2'-deoxyribonucleoside 5'-phosphate Identifier CHEBI:65317 Charge -2 Formula C5H8O6PR SMILEShelp_outline [C@H]1(O[C@H](COP([O-])(=O)[O-])[C@H](C1)O)* 2D coordinates Mol file for the small molecule Search links Involved in 80 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,256 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 2'-deoxyribonucleoside 5'-diphosphate Identifier CHEBI:73316 Charge -3 Formula C5H8O9P2R SMILEShelp_outline O[C@H]1C[C@H]([*])O[C@@H]1COP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 49 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ADP Identifier CHEBI:456216 (Beilstein: 3783669) help_outline Charge -3 Formula C10H12N5O10P2 InChIKeyhelp_outline XTWYTFMLZFPYCI-KQYNXXCUSA-K SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 835 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:11216 | RHEA:11217 | RHEA:11218 | RHEA:11219 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Specific form(s) of this reaction
Publications
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The enzymology of virus-infected bacteria. X. A biochemical-genetic study of the deoxynucleotide kinase induced by wild type and amber mutants of phage T4.
Duckworth D.H., Bessman M.J.
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Identification, cloning, and expression of bacteriophage T5 dnk gene encoding a broad specificity deoxyribonucleoside monophosphate kinase (EC 2.7.4.13).
Mikoulinskaia G.V., Zimin A.A., Feofanov S.A., Miroshnikov A.I.
The nucleotide sequence corresponding to 13-19.5% of the bacteriophage T5 genome in early region C was determined (GenBank AY 140897). One of the five major single-stranded interruptions (nicks) of bacteriophage T5 DNA was identified at 18.5%. The sequenced region was annotated and the putative fu ... >> More
The nucleotide sequence corresponding to 13-19.5% of the bacteriophage T5 genome in early region C was determined (GenBank AY 140897). One of the five major single-stranded interruptions (nicks) of bacteriophage T5 DNA was identified at 18.5%. The sequenced region was annotated and the putative functions of some open reading frames were proposed by comparison with databases. The dnk gene, encoding a deoxyribonucleoside monophosphate kinase, was identified using a previously defined N-terminal amino acid sequence. The gene was cloned and expressed in Escherichia coli, the enzyme was purified to homogeneity with high yield using two alternative methods, and the recombinant deoxyribonucleoside monophosphate kinase was found to have the same activity and specificity as the native enzyme. << Less
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Crystal structure of bacteriophage T4 deoxynucleotide kinase with its substrates dGMP and ATP.
Teplyakov A., Sebastiao P., Obmolova G., Perrakis A., Brush G.S., Bessman M.J., Wilson K.S.
NMP kinases catalyse the phosphorylation of the canonical nucleotides to the corresponding diphosphates using ATP as a phosphate donor. Bacteriophage T4 deoxynucleotide kinase (DNK) is the only member of this family of enzymes that recognizes three structurally dissimilar nucleotides: dGMP, dTMP a ... >> More
NMP kinases catalyse the phosphorylation of the canonical nucleotides to the corresponding diphosphates using ATP as a phosphate donor. Bacteriophage T4 deoxynucleotide kinase (DNK) is the only member of this family of enzymes that recognizes three structurally dissimilar nucleotides: dGMP, dTMP and 5-hydroxymethyl-dCMP while excluding dCMP and dAMP. The crystal structure of DNK with its substrate dGMP has been determined at 2.0 A resolution by single isomorphous replacement. The structure of the ternary complex with dGMP and ATP has been determined at 2.2 A resolution. The polypeptide chain of DNK is folded into two domains of equal size, one of which resembles the mononucleotide binding motif with the glycine-rich P-loop. The second domain, consisting of five alpha-helices, forms the NMP binding pocket. A hinge connection between the domains allows for large movements upon substrate binding which are not restricted by dimerization of the enzyme. The mechanism of active centre formation via domain closure is described. Comparison with other P-loop-containing proteins indicates an induced-fit mode of NTP binding. Protein-substrate interactions observed at the NMP and NTP sites provide the basis for understanding the principles of nucleotide discrimination. << Less
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THE ENZYMOLOGY OF VIRUS-INFECTED BACTERIA. VI. PURIFICATION AND PROPERTIES OF THE DEOXYNUCLEOTIDE KINASE INDUCED BY BACTERIOPHAGE T5.
BESSMAN M.J., HERRIOTT S.T., ORR M.J.