Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline a 3-dehydro-D-guloside Identifier CHEBI:145016 Charge 0 Formula C6H9O6R SMILEShelp_outline [C@@H]1(OC([C@H](O)C([C@H]1O)=O)O*)CO 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 a 3-dehydro-D-glucoside Identifier CHEBI:145017 Charge 0 Formula C6H9O6R SMILEShelp_outline [C@@H]1(OC([C@H](O)C([C@@H]1O)=O)O*)CO 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:61728 | RHEA:61729 | RHEA:61730 | RHEA:61731 | |
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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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Functional Characterization of the ycjQRS Gene Cluster from Escherichia coli: A Novel Pathway for the Transformation of D-Gulosides to D-Glucosides.
Mukherjee K., Huddleston J.P., Narindoshvili T., Nemmara V.V., Raushel F.M.
A combination of bioinformatics, steady-state kinetics, and NMR spectroscopy has revealed the catalytic functions of YcjQ, YcjS, and YcjR from the ycj gene cluster in Escherichia coli K-12. YcjS was determined to be a 3-keto-d-glucoside dehydrogenase with a k<sub>cat</sub> = 22 s<sup>-1</sup> and ... >> More
A combination of bioinformatics, steady-state kinetics, and NMR spectroscopy has revealed the catalytic functions of YcjQ, YcjS, and YcjR from the ycj gene cluster in Escherichia coli K-12. YcjS was determined to be a 3-keto-d-glucoside dehydrogenase with a k<sub>cat</sub> = 22 s<sup>-1</sup> and k<sub>cat</sub>/ K<sub>m</sub> = 2.3 × 10<sup>4</sup> M<sup>-1</sup> s<sup>-1</sup> for the reduction of methyl α-3-keto-d-glucopyranoside at pH 7.0 with NADH. YcjS also exhibited catalytic activity for the NAD<sup>+</sup>-dependent oxidation of d-glucose, methyl β-d-glucopyranoside, and 1,5-anhydro-d-glucitol. YcjQ was determined to be a 3-keto-d-guloside dehydrogenase with k<sub>cat</sub> = 18 s<sup>-1</sup> and k<sub>cat</sub>/ K<sub>m</sub> = 2.0 × 10<sup>3</sup> M<sup>-1</sup> s<sup>-1</sup> for the reduction of methyl α-3-keto-gulopyranoside. This is the first reported dehydrogenase for the oxidation of d-gulose. YcjQ also exhibited catalytic activity with d-gulose and methyl β-d-gulopyranoside. The 3-keto products from both dehydrogenases were found to be extremely labile under alkaline conditions. The function of YcjR was demonstrated to be a C4 epimerase that interconverts 3-keto-d-gulopyranosides to 3-keto-d-glucopyranosides. These three enzymes, YcjQ, YcjR, and YcjS, thus constitute a previously unrecognized metabolic pathway for the transformation of d-gulosides to d-glucosides via the intermediate formation of 3-keto-d-guloside and 3-keto-d-glucoside. << Less
Biochemistry 58:1388-1399(2019) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.