Enzymes
| UniProtKB help_outline | 8,468 proteins |
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Reaction participants Show >> << Hide
- Name help_outline a ribonucleoside 3'-phosphate Identifier CHEBI:13197 Charge -2 Formula C5H8O7PR SMILEShelp_outline [C@@H]1(O[C@H]([C@@H]([C@@H]1OP([O-])(=O)[O-])O)*)CO 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,204 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a ribonucleoside Identifier CHEBI:18254 Charge 0 Formula C5H9O4R SMILEShelp_outline OC[C@H]1O[C@@H]([*])[C@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 210 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline phosphate Identifier CHEBI:43474 Charge -2 Formula HO4P InChIKeyhelp_outline NBIIXXVUZAFLBC-UHFFFAOYSA-L SMILEShelp_outline OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 992 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:10144 | RHEA:10145 | RHEA:10146 | RHEA:10147 | |
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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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Purification and characterization of yfkN, a trifunctional nucleotide phosphoesterase secreted by Bacillus subtilis.
Chambert R., Pereira Y., Petit-Glatron M.-F.
YfkN isolated from the culture supernatant of Bacillus subtilis in the exponential phase of growth is a protein of 143.5 kDa that derives from a putative large precursor of 159.6 kDa processed at both the N- and C-terminal ends. Pulse-chase experiments indicated that the release occurs slowly with ... >> More
YfkN isolated from the culture supernatant of Bacillus subtilis in the exponential phase of growth is a protein of 143.5 kDa that derives from a putative large precursor of 159.6 kDa processed at both the N- and C-terminal ends. Pulse-chase experiments indicated that the release occurs slowly with a half-time longer than 30 min, suggesting that the event is coupled with wall turnover. YfkN exhibits 2',3' cyclic nucleotide phosphodiesterase, 2' (or 3') nucleotidase and 5' nucleotidase activities. In vitro the protein is reduced by subtilisin digestion to a shorter polypeptide (68 kDa), displaying phosphodiesterase activity but devoid of any 5'nucleotidase activity. This proteolytic processing led us to localize the potential active sites of the various nucleotidase activities. When bacteria were grown in low phosphate medium, the exocellular production of the enzyme was enhanced, suggesting that it plays a role in phosphate metabolism. Comparison with nucleotidase databases suggests that yfkN resulted from gene fusion. << Less
J. Biochem. 134:655-660(2003) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.