Reaction participants Show >> << Hide
- Name help_outline a ribonucleoside 5'-diphosphate Identifier CHEBI:57930 Charge -3 Formula C5H8O10P2R SMILEShelp_outline [C@H]1([C@H]([C@@H](O)[C@@H](O1)*)O)COP(OP([O-])(=O)[O-])(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 1,644 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline GTP Identifier CHEBI:37565 (Beilstein: 5211792) help_outline Charge -4 Formula C10H12N5O14P3 InChIKeyhelp_outline XKMLYUALXHKNFT-UUOKFMHZSA-J SMILEShelp_outline Nc1nc2n(cnc2c(=O)[nH]1)[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 94 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a ribonucleoside 5'-triphosphate Identifier CHEBI:61557 Charge -4 Formula C5H8O13P3R SMILEShelp_outline [C@H]1([C@H]([C@@H](O)[C@@H](O1)*)O)COP(OP(OP(=O)([O-])[O-])(=O)[O-])(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 1,505 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline GDP Identifier CHEBI:58189 Charge -3 Formula C10H12N5O11P2 InChIKeyhelp_outline QGWNDRXFNXRZMB-UUOKFMHZSA-K SMILEShelp_outline Nc1nc2n(cnc2c(=O)[nH]1)[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 184 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:79879 | RHEA:79880 | RHEA:79881 | RHEA:79882 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
Specific form(s) of this reaction
Publications
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The human adenylate kinase 9 is a nucleoside mono- and diphosphate kinase.
Amiri M., Conserva F., Panayiotou C., Karlsson A., Solaroli N.
Adenylate kinases regulate adenine nucleotide levels and are present in different intracellular compartments. These enzymes also participate in the activation of pharmacologically active nucleoside and nucleotide analogs. We have in the present study identified the ninth isoform of the adenylate k ... >> More
Adenylate kinases regulate adenine nucleotide levels and are present in different intracellular compartments. These enzymes also participate in the activation of pharmacologically active nucleoside and nucleotide analogs. We have in the present study identified the ninth isoform of the adenylate kinase family of enzymes and accordingly named the protein adenylate kinase 9 (AK9). Initially a full-length cDNA of a hypothetical protein containing a predicted adenylate kinase domain was identified and subsequently cloned and expressed in Escherichia coli. The substrate specificity of the recombinant protein showed that the enzyme catalyzed the phosphorylation of AMP, dAMP, CMP and dCMP with ATP as phosphate donor, while only AMP and CMP were phosphorylated when GTP was the phosphate donor. The kinetic parameters of AK9 were determined for AMP, dAMP and CMP with ATP as phosphate donor. Interestingly, in addition to the diphosphate products, a nucleoside diphosphate kinase (NDPK) activity was also present with subsequent triphosphates formed. With ATP or GTP as phosphate donor it was possible to detect the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and TTP as enzymatic products from the corresponding diphosphate substrates. A number of previously characterized adenylate kinases were also tested and found to possess a broad phosphotransferase activity similar to AK9. These enzymes are accordingly suggested to be regarded as nucleoside mono- and diphosphate kinases with catalytic activities possibly determined by local substrate concentrations. << Less
Int. J. Biochem. Cell Biol. 45:925-931(2013) [PubMed] [EuropePMC]
This publication is cited by 23 other entries.