Enzymes
| UniProtKB help_outline | 1 proteins |
| Enzyme class help_outline |
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- Name help_outline L-galactonate Identifier CHEBI:53071 (Beilstein: 3906527) help_outline Charge -1 Formula C6H11O7 InChIKeyhelp_outline RGHNJXZEOKUKBD-RSJOWCBRSA-M SMILEShelp_outline OC[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NAD+ Identifier CHEBI:57540 (Beilstein: 3868403) help_outline Charge -1 Formula C21H26N7O14P2 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,186 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 keto-D-tagaturonate Identifier CHEBI:17886 (Beilstein: 3907133) help_outline Charge -1 Formula C6H9O7 InChIKeyhelp_outline IZSRJDGCGRAUAR-WDCZJNDASA-M SMILEShelp_outline OCC(=O)[C@@H](O)[C@@H](O)[C@H](O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline NADH Identifier CHEBI:57945 (Beilstein: 3869564) help_outline Charge -2 Formula C21H27N7O14P2 InChIKeyhelp_outline BOPGDPNILDQYTO-NNYOXOHSSA-L SMILEShelp_outline NC(=O)C1=CN(C=CC1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,116 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:30183 | RHEA:30184 | RHEA:30185 | RHEA:30186 | |
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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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The pathway for L-galactonate catabolism in Escherichia coli K-12.
Cooper R.A.
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l-Galactose metabolism in Bacteroides vulgatus from the human gut microbiota.
Hobbs M.E., Williams H.J., Hillerich B., Almo S.C., Raushel F.M.
A previously unknown metabolic pathway for the utilization of l-galactose was discovered in a prevalent gut bacterium, Bacteroides vulgatus. The new pathway consists of three previously uncharacterized enzymes that were found to be responsible for the conversion of l-galactose to d-tagaturonate. B ... >> More
A previously unknown metabolic pathway for the utilization of l-galactose was discovered in a prevalent gut bacterium, Bacteroides vulgatus. The new pathway consists of three previously uncharacterized enzymes that were found to be responsible for the conversion of l-galactose to d-tagaturonate. Bvu0219 (l-galactose dehydrogenase) was determined to oxidize l-galactose to l-galactono-1,5-lactone with kcat and kcat/Km values of 21 s(-1) and 2.0 × 10(5) M(-1) s(-1), respectively. The kinetic product of Bvu0219 is rapidly converted nonenzymatically to the thermodynamically more stable l-galactono-1,4-lactone. Bvu0220 (l-galactono-1,5-lactonase) hydrolyzes both the kinetic and thermodynamic products of Bvu0219 to l-galactonate. However, l-galactono-1,5-lactone is estimated to be hydrolyzed 300-fold faster than its thermodynamically more stable counterpart, l-galactono-1,4-lactone. In the final step of this pathway, Bvu0222 (l-galactonate dehydrogenase) oxidizes l-galactonate to d-tagaturonate with kcat and kcat/Km values of 0.6 s(-1) and 1.7 × 10(4) M(-1) s(-1), respectively. In the reverse direction, d-tagaturonate is reduced to l-galactonate with values of kcat and kcat/Km of 90 s(-1) and 1.6 × 10(5) M(-1) s(-1), respectively. d-Tagaturonate is subsequently converted to d-glyceraldehyde and pyruvate through enzymes encoded within the degradation pathway for d-glucuronate and d-galacturonate. << Less
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The yjjN of E. coli codes for an L-galactonate dehydrogenase and can be used for quantification of L-galactonate and L-gulonate.
Kuivanen J., Richard P.
Escherichia coli is able to utilize L-galactonate as a sole carbon source. A metabolic pathway for L-galactonate catabolism is described in E. coli, and it is known to be interconnected with D-galacturonate metabolism. The corresponding gene encoding the first enzyme in the L-galactonate pathway, ... >> More
Escherichia coli is able to utilize L-galactonate as a sole carbon source. A metabolic pathway for L-galactonate catabolism is described in E. coli, and it is known to be interconnected with D-galacturonate metabolism. The corresponding gene encoding the first enzyme in the L-galactonate pathway, L-galactonate-5-dehydrogenase, was suggested to be yjjN. However, L-galactonate dehydrogenase activity was never demonstrated with the yjjN gene product. Here, we show that YjjN is indeed an L-galactonate dehydrogenase having activity also for L-gulonate. The K m and k cat for L-galactonate were 19.5±0.6 mM and 0.51±0.03 s(-1), respectively. In addition, YjjN was applied for a quantitative detection of the both of these substances in a coupled assay. The detection limits for L-galactonate and L-gulonate were 1.65 and 10 μM, respectively. << Less
Appl. Biochem. Biotechnol. 173:1829-1835(2014) [PubMed] [EuropePMC]