Reaction participants Show >> << Hide
- Name help_outline (2S)-2-phospholactate Identifier CHEBI:59906 (Beilstein: 3669296) help_outline Charge -3 Formula C3H4O6P InChIKeyhelp_outline CSZRNWHGZPKNKY-REOHCLBHSA-K SMILEShelp_outline C[C@H](OP([O-])([O-])=O)C([O-])=O 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 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 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2S)-lactyl-2-diphospho-5'-guanosine Identifier CHEBI:59435 Charge -3 Formula C13H16N5O13P2 InChIKeyhelp_outline JAIRGSHHKMPRGE-LJRSMJOYSA-K SMILEShelp_outline C[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n1cnc2c1nc(N)[nH]c2=O)C([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 1,129 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:63424 | RHEA:63425 | RHEA:63426 | RHEA:63427 | |
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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.
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A revised biosynthetic pathway for the cofactor F420 in prokaryotes.
Bashiri G., Antoney J., Jirgis E.N.M., Shah M.V., Ney B., Copp J., Stuteley S.M., Sreebhavan S., Palmer B., Middleditch M., Tokuriki N., Greening C., Scott C., Baker E.N., Jackson C.J.
Cofactor F<sub>420</sub> plays critical roles in primary and secondary metabolism in a range of bacteria and archaea as a low-potential hydride transfer agent. It mediates a variety of important redox transformations involved in bacterial persistence, antibiotic biosynthesis, pro-drug activation a ... >> More
Cofactor F<sub>420</sub> plays critical roles in primary and secondary metabolism in a range of bacteria and archaea as a low-potential hydride transfer agent. It mediates a variety of important redox transformations involved in bacterial persistence, antibiotic biosynthesis, pro-drug activation and methanogenesis. However, the biosynthetic pathway for F<sub>420</sub> has not been fully elucidated: neither the enzyme that generates the putative intermediate 2-phospho-L-lactate, nor the function of the FMN-binding C-terminal domain of the γ-glutamyl ligase (FbiB) in bacteria are known. Here we present the structure of the guanylyltransferase FbiD and show that, along with its archaeal homolog CofC, it accepts phosphoenolpyruvate, rather than 2-phospho-L-lactate, as the substrate, leading to the formation of the previously uncharacterized intermediate dehydro-F<sub>420</sub>-0. The C-terminal domain of FbiB then utilizes FMNH<sub>2</sub> to reduce dehydro-F<sub>420</sub>-0, which produces mature F<sub>420</sub> species when combined with the γ-glutamyl ligase activity of the N-terminal domain. These new insights have allowed the heterologous production of F<sub>420</sub> from a recombinant F<sub>420</sub> biosynthetic pathway in Escherichia coli. << Less
Nat. Commun. 10:1558-1558(2019) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.