Reaction participants Show >> << Hide
- Name help_outline dUMP Identifier CHEBI:246422 (Beilstein: 4011255) help_outline Charge -2 Formula C9H11N2O8P InChIKeyhelp_outline JSRLJPSBLDHEIO-SHYZEUOFSA-L SMILEShelp_outline O[C@H]1C[C@@H](O[C@@H]1COP([O-])([O-])=O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 13 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 1,301 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline dUDP Identifier CHEBI:60471 Charge -3 Formula C9H11N2O11P2 InChIKeyhelp_outline QHWZTVCCBMIIKE-SHYZEUOFSA-K SMILEShelp_outline O[C@H]1C[C@@H](O[C@@H]1COP([O-])(=O)OP([O-])([O-])=O)n1ccc(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 5 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 854 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:30655 | RHEA:30656 | RHEA:30657 | RHEA:30658 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Molecular characterization of <i>Drosophila melanogaster</i> thymidylate kinase.
Hu Frisk J., Wang L.
<i>Drosophila</i> has been used as an animal model to study pathogenic mechanism of neurological disorders. Thymidylate kinase (TMPK) is an essential enzyme in dTTP synthesis catalyzing the phosphorylation of dTMP to dTDP. Loss of function mutations in the <i>DTYMK</i> gene, coding for TMPK, cause ... >> More
<i>Drosophila</i> has been used as an animal model to study pathogenic mechanism of neurological disorders. Thymidylate kinase (TMPK) is an essential enzyme in dTTP synthesis catalyzing the phosphorylation of dTMP to dTDP. Loss of function mutations in the <i>DTYMK</i> gene, coding for TMPK, cause severe microcephaly in human patients. In this study, <i>Drosophila melanogaster</i> TMPK (DmTMPK) was cloned, expressed, purified and characterized. Unlike human TMPK, DmTMPK phosphorylated not only dTMP and dUMP but also dGMP and dIMP although with low efficiency. ATP and dATP are the most efficient phosphate donor but at higher concentration (>1 mM) ATP inhibited DmTMPK activity. Sequence and structural model analysis explain why DmTMPK could phosphorylate purine nucleoside monophosphates. This study has laid a solid foundation for future study of TMPK function in <i>Drosophila</i>. << Less
Nucleosides Nucleotides Nucleic Acids 43:734-742(2024) [PubMed] [EuropePMC]
This publication is cited by 6 other entries.