Enzymes
UniProtKB help_outline | 1,300 proteins |
Enzyme class help_outline |
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- 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 keto-D-fructuronate Identifier CHEBI:59881 (Beilstein: 4138715) help_outline Charge -1 Formula C6H9O7 InChIKeyhelp_outline IZSRJDGCGRAUAR-WISUUJSJSA-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 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:51656 | RHEA:51657 | RHEA:51658 | RHEA:51659 | |
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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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Tagaturonate-fructuronate epimerase UxaE, a novel enzyme in the hexuronate catabolic network in Thermotoga maritima.
Rodionova I.A., Scott D.A., Grishin N.V., Osterman A.L., Rodionov D.A.
Thermotoga maritima is a marine hyperthermophilic microorganism that degrades a wide range of simple and complex carbohydrates including pectin and produces fermentative hydrogen at high yield. Galacturonate and glucuronate, two abundant hexuronic acids in pectin and xylan, respectively, are catab ... >> More
Thermotoga maritima is a marine hyperthermophilic microorganism that degrades a wide range of simple and complex carbohydrates including pectin and produces fermentative hydrogen at high yield. Galacturonate and glucuronate, two abundant hexuronic acids in pectin and xylan, respectively, are catabolized via committed metabolic pathways to supply carbon and energy for a variety of microorganisms. By a combination of bioinformatics and experimental techniques we identified a novel enzyme family (named UxaE) catalysing a previously unknown reaction in the hexuronic acid catabolic pathway, epimerization of tagaturonate to fructuronate. The enzymatic activity of the purified recombinant tagaturonate epimerase from T. maritima was directly confirmed and kinetically characterized. Its function was also confirmed by genetic complementation of the growth of the Escherichia coli uxaB knockout mutant strain on galacturonate. An inferred novel galacturonate to mannonate catabolic pathway in T. maritima was reconstituted in vitro using a mixture of recombinant purified enzymes UxaE, UxaC and UxuB. Members of the newly identified UxaE family were identified in ~50 phylogenetically diverse heterotrophic bacteria from aquatic and soil environments. The genomic context of respective genes and reconstruction of associated pathways suggest that UxaE enzymatic and biological function remains conserved in all of these species. << Less