Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline 2-hydroxyethylphosphonate Identifier CHEBI:60991 Charge -1 Formula C2H6O4P InChIKeyhelp_outline SEHJHHHUIGULEI-UHFFFAOYSA-M SMILEShelp_outline OCCP(O)([O-])=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 CTP Identifier CHEBI:37563 (Beilstein: 4732530) help_outline Charge -4 Formula C9H12N3O14P3 InChIKeyhelp_outline PCDQPRRSZKQHHS-XVFCMESISA-J SMILEShelp_outline Nc1ccn([C@@H]2O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]2O)c(=O)n1 2D coordinates Mol file for the small molecule Search links Involved in 82 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline cytidine 5'-{[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate} Identifier CHEBI:142876 Charge -2 Formula C11H17N3O11P2 InChIKeyhelp_outline ODFOOQGQRDVSPW-PEBGCTIMSA-L SMILEShelp_outline O(P(=O)([O-])OC[C@H]1O[C@@H](N2C=CC(=NC2=O)N)[C@@H]([C@@H]1O)O)P(=O)([O-])CCO 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 diphosphate Identifier CHEBI:33019 (Beilstein: 185088) help_outline Charge -3 Formula HO7P2 InChIKeyhelp_outline XPPKVPWEQAFLFU-UHFFFAOYSA-K SMILEShelp_outline OP([O-])(=O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1,139 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:63420 | RHEA:63421 | RHEA:63422 | RHEA:63423 | |
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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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Fosfomycin biosynthesis via transient cytidylylation of 2-hydroxyethylphosphonate by the bifunctional Fom1 enzyme.
Cho S.H., Kim S.Y., Tomita T., Shiraishi T., Park J.S., Sato S., Kudo F., Eguchi T., Funa N., Nishiyama M., Kuzuyama T.
Fosfomycin is a wide-spectrum phosphonate antibiotic that is used clinically to treat cystitis, tympanitis, etc. Its biosynthesis starts with the formation of a carbon-phosphorus bond catalyzed by the phosphoenolpyruvate phosphomutase Fom1. We identified an additional cytidylyltransferase (CyTase) ... >> More
Fosfomycin is a wide-spectrum phosphonate antibiotic that is used clinically to treat cystitis, tympanitis, etc. Its biosynthesis starts with the formation of a carbon-phosphorus bond catalyzed by the phosphoenolpyruvate phosphomutase Fom1. We identified an additional cytidylyltransferase (CyTase) domain at the Fom1 N-terminus in addition to the phosphoenolpyruvate phosphomutase domain at the Fom1 C-terminus. Here, we demonstrate that Fom1 is bifunctional and that the Fom1 CyTase domain catalyzes the cytidylylation of the 2-hydroxyethylphosphonate (HEP) intermediate to produce cytidylyl-HEP. On the basis of this new function of Fom1, we propose a revised fosfomycin biosynthetic pathway that involves the transient CMP-conjugated intermediate. The identification of a biosynthetic mechanism via such transient cytidylylation of a biosynthetic intermediate fundamentally advances the understanding of phosphonate biosynthesis in nature. The crystal structure of the cytidylyl-HEP-bound CyTase domain provides a basis for the substrate specificity and reveals unique catalytic elements not found in other members of the CyTase family. << Less