Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline (2R)-3-phosphoglycerate Identifier CHEBI:58272 Charge -3 Formula C3H4O7P InChIKeyhelp_outline OSJPPGNTCRNQQC-UWTATZPHSA-K SMILEShelp_outline O[C@H](COP([O-])([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 24 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 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 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 3-[(R)-glyceryl]-diphospho-5'-guanosine Identifier CHEBI:147306 Charge -3 Formula C13H16N5O14P2 InChIKeyhelp_outline UBONPDGCIQEDRL-QWEIRQIHSA-K SMILEShelp_outline O(P(OP(=O)(OC[C@@H]1[C@H]([C@H]([C@H](N2C=3N=C(NC(C3N=C2)=O)N)O1)O)O)[O-])([O-])=O)C[C@H](C([O-])=O)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 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:63440 | RHEA:63441 | RHEA:63442 | RHEA:63443 | |
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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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Metabolic pathway rerouting in Paraburkholderia rhizoxinica evolved long-overlooked derivatives of coenzyme F420.
Braga D., Last D., Hasan M., Guo H., Leichnitz D., Uzum Z., Richter I., Schalk F., Beemelmanns C., Hertweck C., Lackner G.
Coenzyme F<sub>420</sub> is a specialized redox cofactor with a negative redox potential. It supports biochemical processes like methanogenesis, degradation of xenobiotics, and the biosynthesis of antibiotics. Although well-studied in methanogenic archaea and actinobacteria, not much is known abou ... >> More
Coenzyme F<sub>420</sub> is a specialized redox cofactor with a negative redox potential. It supports biochemical processes like methanogenesis, degradation of xenobiotics, and the biosynthesis of antibiotics. Although well-studied in methanogenic archaea and actinobacteria, not much is known about F<sub>420</sub> in Gram-negative bacteria. Genome sequencing revealed F<sub>420</sub> biosynthetic genes in the Gram-negative, endofungal bacterium <i>Paraburkholderia rhizoxinica</i>, a symbiont of phytopathogenic fungi. Fluorescence microscopy, high-resolution LC-MS, and structure elucidation by NMR demonstrated that the encoded pathway is active and yields unexpected derivatives of F<sub>420</sub> (3PG-F<sub>420</sub>). Further analyses of a biogas-producing microbial community showed that these derivatives are more widespread in nature. Genetic and biochemical studies of their biosynthesis established that a specificity switch in the guanylyltransferase CofC reprogrammed the pathway to start from 3-phospho-d-glycerate, suggesting a rerouting event during the evolution of F<sub>420</sub> biosynthesis. Furthermore, the cofactor activity of 3PG-F<sub>420</sub> was validated, thus opening up perspectives for its use in biocatalysis. The 3PG-F<sub>420</sub> biosynthetic gene cluster is fully functional in <i>Escherichia coli</i>, enabling convenient production of the cofactor by fermentation. << Less
ACS Chem. Biol. 14:2088-2094(2019) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.