Enzymes
| UniProtKB help_outline | 12 proteins |
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- Name help_outline 2-dehydro-3-deoxy-D-gluconate Identifier CHEBI:57990 Charge -1 Formula C6H9O6 InChIKeyhelp_outline WPAMZTWLKIDIOP-WVZVXSGGSA-M SMILEShelp_outline OC[C@@H](O)[C@@H](O)CC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 11 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 2-dehydro-3-deoxy-6-phospho-D-gluconate Identifier CHEBI:57569 (Beilstein: 6714585) help_outline Charge -3 Formula C6H8O9P InChIKeyhelp_outline OVPRPPOVAXRCED-WVZVXSGGSA-K SMILEShelp_outline O[C@H](COP([O-])([O-])=O)[C@@H](O)CC(=O)C([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 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:14797 | RHEA:14798 | RHEA:14799 | RHEA:14800 | |
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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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Prediction of enzymatic pathways by integrative pathway mapping.
Calhoun S., Korczynska M., Wichelecki D.J., San Francisco B., Zhao S., Rodionov D.A., Vetting M.W., Al-Obaidi N.F., Lin H., O'Meara M.J., Scott D.A., Morris J.H., Russel D., Almo S.C., Osterman A.L., Gerlt J.A., Jacobson M.P., Shoichet B.K., Sali A.
The functions of most proteins are yet to be determined. The function of an enzyme is often defined by its interacting partners, including its substrate and product, and its role in larger metabolic networks. Here, we describe a computational method that predicts the functions of orphan enzymes by ... >> More
The functions of most proteins are yet to be determined. The function of an enzyme is often defined by its interacting partners, including its substrate and product, and its role in larger metabolic networks. Here, we describe a computational method that predicts the functions of orphan enzymes by organizing them into a linear metabolic pathway. Given candidate enzyme and metabolite pathway members, this aim is achieved by finding those pathways that satisfy structural and network restraints implied by varied input information, including that from virtual screening, chemoinformatics, genomic context analysis, and ligand -binding experiments. We demonstrate this integrative pathway mapping method by predicting the L-gulonate catabolic pathway in <i>Haemophilus influenzae</i> Rd KW20. The prediction was subsequently validated experimentally by enzymology, crystallography, and metabolomics. Integrative pathway mapping by satisfaction of structural and network restraints is extensible to molecular networks in general and thus formally bridges the gap between structural biology and systems biology. << Less
Elife 7:e31097-e31097(2018) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.
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Promiscuity in the part-phosphorylative Entner-Doudoroff pathway of the archaeon Sulfolobus solfataricus.
Lamble H.J., Theodossis A., Milburn C.C., Taylor G.L., Bull S.D., Hough D.W., Danson M.J.
The hyperthermophilic archaeon Sulfolobus solfataricus metabolises glucose and galactose by a 'promiscuous' non-phosphorylative variant of the Entner-Doudoroff pathway, in which a series of enzymes have sufficient substrate promiscuity to permit the metabolism of both sugars. Recently, it has been ... >> More
The hyperthermophilic archaeon Sulfolobus solfataricus metabolises glucose and galactose by a 'promiscuous' non-phosphorylative variant of the Entner-Doudoroff pathway, in which a series of enzymes have sufficient substrate promiscuity to permit the metabolism of both sugars. Recently, it has been proposed that the part-phosphorylative Entner-Doudoroff pathway occurs in parallel in S. solfataricus as an alternative route for glucose metabolism. In this report we demonstrate, by in vitro kinetic studies of D-2-keto-3-deoxygluconate (KDG) kinase and KDG aldolase, that the part-phosphorylative pathway in S. solfataricus is also promiscuous for the metabolism of both glucose and galactose. << Less
FEBS Lett. 579:6865-6869(2005) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Uronic acid metabolism in bacteria. IV. Purification and properties of 2-keto-3-deoxy-D-gluconokinase in Escherichia coli.
Cynkin M.A., Ashwell G.
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Characterization of Sulfolobus solfataricus 2-keto-3-deoxy-D-gluconate kinase in the modified Entner-Doudoroff pathway.
Kim S., Lee S.B.
The thermoacidophilic archaeon Sulfolobus solfataricus is known to utilize D-glucose via the nonphosphorylated Entner-Doudoroff (ED) pathway. But, the genome database shows that this microorganism has a gene (kdgK) encoding 2-keto-3-deoxy-D-gluconate (KDG) kinase (KDGK) which phosphorylates KDG to ... >> More
The thermoacidophilic archaeon Sulfolobus solfataricus is known to utilize D-glucose via the nonphosphorylated Entner-Doudoroff (ED) pathway. But, the genome database shows that this microorganism has a gene (kdgK) encoding 2-keto-3-deoxy-D-gluconate (KDG) kinase (KDGK) which phosphorylates KDG to 2-keto-3-deoxy-6-phosphogluconate. Interestingly, kdgK and three other genes in the modified ED pathway are organized as an operon-like structure. In this study, we report confirmation of the catalytic activity of the S. solfataricus KDGK protein. We also found that the kdgK gene was transcribed as polycistronic transcripts. Proteome analysis of cell lysate revealed that all gene products in the kdgK operon were expressed as functional proteins. These results strongly indicate that S. solfataricus metabolizes D-glucose via the 'partially' nonphosphorylated ED pathway. A purified recombinant S. solfataricus KDGK had K(m) and k(cat) values of 0.14 mM and 60.8 s(-1) respectively for KDG, and showed maximal activity at temperatures between 70 and 80 degrees C and pHs between 7.0 and 8.0. << Less
Biosci. Biotechnol. Biochem. 70:1308-1316(2006) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.