Enzymes
| UniProtKB help_outline | 3 proteins |
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| GO Molecular Function help_outline |
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- Name help_outline pseudouridine Identifier CHEBI:17802 (Beilstein: 32779; CAS: 1445-07-4) help_outline Charge 0 Formula C9H12N2O6 InChIKeyhelp_outline PTJWIQPHWPFNBW-GBNDHIKLSA-N SMILEShelp_outline OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)c1c[nH]c(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 2 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 ψ-UMP Identifier CHEBI:58380 Charge -2 Formula C9H11N2O9P InChIKeyhelp_outline MOBMOJGXNHLLIR-GBNDHIKLSA-L SMILEShelp_outline O[C@@H]1[C@@H](COP([O-])([O-])=O)O[C@H]([C@@H]1O)c1c[nH]c(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 4 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
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,717 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:22448 | RHEA:22449 | RHEA:22450 | RHEA:22451 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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STUDIES ON THE BIOSYNTHESIS OF 5-RIBOSYLURACIL 5'-MONOPHOSPHATE IN TETRAHYMENA PYRIFORMIS.
HEINRIKSON R.L., GOLDWASSER E.
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Enzymatic synthesis of deoxypseudouridylic acid and a study of certain of its properties.
Remsen J.F., Matsushita T., Chirikjian J.G., Davis F.F.
Biochim Biophys Acta 281:481-487(1972) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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On the biosynthesis of pseudouridine and of pseudouridylic acid in Agrobacterium tumefaciens.
Suzuki T., Hochster R.M.
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Molecular identification of pseudouridine-metabolizing enzymes.
Preumont A., Snoussi K., Stroobant V., Collet J.-F., Van Schaftingen E.
Pseudouridine, a non-classical nucleoside present in human urine as a degradation product of RNAs, is one of the few molecules that has a glycosidic C-C bond. Through a data base mining approach involving transcriptomic data, we have molecularly identified two enzymes that are involved in the meta ... >> More
Pseudouridine, a non-classical nucleoside present in human urine as a degradation product of RNAs, is one of the few molecules that has a glycosidic C-C bond. Through a data base mining approach involving transcriptomic data, we have molecularly identified two enzymes that are involved in the metabolism of pseudouridine in uropathogenic Escherichia coli, the principal agent of urinary tract infections in humans. The first enzyme, coded by the gene yeiC, specifically phosphorylates pseudouridine to pseudouridine 5'-phosphate. Accordingly, yeiC(-) mutants are unable to metabolize pseudouridine, in contrast to wild-type E. coli UTI89. The second enzyme, encoded by the gene yeiN belonging to the same operon as yeiC, catalyzes the conversion of pseudouridine 5'-phosphate to uracil and ribose 5-phosphate in a divalent cation-dependent manner. Remarkably, the glycosidic C-C bond of pseudouridine is cleaved in the course of this reaction, indicating that YeiN is the first molecularly identified enzyme able to hydrolyze a glycosidic C-C bond. Though this reaction is easily reversible, the association of YeiN with pseudouridine kinase indicates that it serves physiologically to metabolize pseudouridine 5'-phosphate rather than to form it. YeiN is homologous to Thermotoga maritima IndA, a protein with a new fold, which we now show to act also as a pseudouridine-5'-phosphate glycosidase. Data base mining indicates that most eukaryotes possess homologues of pseudouridine kinase and pseudouridine-5'-phosphate glycosidase and that these are most often associated in a single bifunctional protein. The gene encoding this bifunctional protein is absent from the genomes of man and other mammals, indicating that the capacity for metabolizing pseudouridine has been lost late in evolution. << Less
J. Biol. Chem. 283:25238-25246(2008) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.