Enzymes
| UniProtKB help_outline | 2 proteins |
| Enzyme class help_outline |
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Reaction participants Show >> << Hide
- Name help_outline 3,6-anhydro-L-galactonate Identifier CHEBI:83435 Charge -1 Formula C6H9O6 InChIKeyhelp_outline ZDDQAAZBPZGPRB-SKNVOMKLSA-M SMILEShelp_outline O[C@@H]([C@@H]1OC[C@H](O)[C@H]1O)C([O-])=O 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
- Name help_outline 2-dehydro-3-deoxy-L-galactonate Identifier CHEBI:75545 Charge -1 Formula C6H9O6 InChIKeyhelp_outline WPAMZTWLKIDIOP-UCORVYFPSA-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 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:21512 | RHEA:21513 | RHEA:21514 | RHEA:21515 | |
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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 novel catabolic pathway of 3,6-anhydro-L-galactose, the main component of red macroalgae, in a marine bacterium.
Yun E.J., Lee S., Kim H.T., Pelton J.G., Kim S., Ko H.J., Choi I.G., Kim K.H.
The catabolic fate of the major monomeric sugar of red macroalgae, 3,6-anhydro-L-galactose (AHG), is completely unknown in any organisms. AHG is not catabolized by ordinary fermentative microorganisms, and it hampers the utilization of red macroalgae as renewable biomass for biofuel and chemical p ... >> More
The catabolic fate of the major monomeric sugar of red macroalgae, 3,6-anhydro-L-galactose (AHG), is completely unknown in any organisms. AHG is not catabolized by ordinary fermentative microorganisms, and it hampers the utilization of red macroalgae as renewable biomass for biofuel and chemical production. In this study, metabolite and transcriptomic analyses of Vibrio sp., a marine bacterium capable of catabolizing AHG as a sole carbon source, revealed two key metabolic intermediates of AHG, 3,6-anhydrogalactonate (AHGA) and 2-keto-3-deoxy-galactonate; the corresponding genes were verified in vitro enzymatic reactions using their recombinant proteins. Oxidation by an NADP(+) -dependent AHG dehydrogenase and isomerization by an AHGA cycloisomerase are the two key AHG metabolic processes. This newly discovered metabolic route was verified in vivo by demonstrating the growth of Escherichia coli harbouring the genes of these two enzymes on AHG as a sole carbon source. Also, the introduction of only these two enzymes into an ethanologenic E. coli strain increased the ethanol production in E. coli by fermenting both AHG and galactose in an agarose hydrolysate. These findings provide not only insights for the evolutionary adaptation of a central metabolic pathway to utilize uncommon substrates in microbes, but also a metabolic design principle for bioconversion of red macroalgal biomass into biofuels or industrial chemicals. << Less
Environ. Microbiol. 17:1677-1688(2015) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
Comments
Published in: "Metabolic pathway of 3,6-anhydro-L-galactose in agar-degrading microorganisms." Lee SB, Cho SJ, Kim JA, Lee SY, Kim SM, Lim HS. Biotechnology and Bioprocess Engineering 19(5);866-878 (2014).