Enzymes
| UniProtKB help_outline | 1 proteins |
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Reaction participants Show >> << Hide
- Name help_outline D-galactaro-1,5-lactone Identifier CHEBI:83383 Charge -1 Formula C6H7O7 InChIKeyhelp_outline YLKFQNUGXOLRNI-KXMYSMCESA-M SMILEShelp_outline O[C@H]1[C@@H](O)[C@H](OC(=O)[C@@H]1O)C([O-])=O 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 D-galactaro-1,4-lactone Identifier CHEBI:85317 Charge -1 Formula C6H7O7 InChIKeyhelp_outline XECPAIJNBXCOBO-LKELSTGYSA-M SMILEShelp_outline O[C@@H]([C@@H]1OC(=O)[C@H](O)[C@H]1O)C([O-])=O 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
Cross-references
| RHEA:45580 | RHEA:45581 | RHEA:45582 | RHEA:45583 | |
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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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Galactaro delta-lactone isomerase: lactone isomerization by a member of the amidohydrolase superfamily.
Bouvier J.T., Groninger-Poe F.P., Vetting M., Almo S.C., Gerlt J.A.
Agrobacterium tumefaciens strain C58 can utilize d-galacturonate as a sole source of carbon via a pathway in which the first step is oxidation of d-galacturonate to D-galactaro-1,5-lactone. We have identified a novel enzyme, D-galactarolactone isomerase (GLI), that catalyzes the isomerizaton of D- ... >> More
Agrobacterium tumefaciens strain C58 can utilize d-galacturonate as a sole source of carbon via a pathway in which the first step is oxidation of d-galacturonate to D-galactaro-1,5-lactone. We have identified a novel enzyme, D-galactarolactone isomerase (GLI), that catalyzes the isomerizaton of D-galactaro-1,5-lactone to D-galactaro-1,4-lactone. GLI, a member of the functionally diverse amidohydrolase superfamily, is a homologue of LigI that catalyzes the hydrolysis of 2-pyrone-4,6-dicarboxylate in lignin degradation. The ability of GLI to catalyze lactone isomerization instead of hydrolysis can be explained by the absence of the general basic catalysis used by 2-pyrone-4,6-dicarboxylate lactonase. << Less
Biochemistry 53:614-616(2014) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.