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TitleMolecular basis of sulfolactate synthesis by sulfolactaldehyde dehydrogenase from .
Journal, issue, pagesChem Sci, Vol. 14, Issue 41, Page 11429-11440, Year 2023
Publish dateOct 25, 2023
AuthorsJinling Li / Mahima Sharma / Richard Meek / Amani Alhifthi / Zachary Armstrong / Niccolay Madiedo Soler / Mihwa Lee / Ethan D Goddard-Borger / James N Blaza / Gideon J Davies / Spencer J Williams /
PubMed AbstractSulfolactate (SL) is a short-chain organosulfonate that is an important reservoir of sulfur in the biosphere. SL is produced by oxidation of sulfolactaldehyde (SLA), which in turn derives from ...Sulfolactate (SL) is a short-chain organosulfonate that is an important reservoir of sulfur in the biosphere. SL is produced by oxidation of sulfolactaldehyde (SLA), which in turn derives from sulfoglycolysis of the sulfosugar sulfoquinovose, or through oxidation of 2,3-dihydroxypropanesulfonate. Oxidation of SLA is catalyzed by SLA dehydrogenases belonging to the aldehyde dehydrogenase superfamily. We report that SLA dehydrogenase GabD from the sulfoglycolytic bacterium SRDI565 can use both NAD and NADP as cofactor to oxidize SLA, and indicatively operates through a rapid equilibrium ordered mechanism. We report the cryo-EM structure of GabD bound to NADH, revealing a tetrameric quaternary structure and supporting proposal of organosulfonate binding residues in the active site, and a catalytic mechanism. Sequence based homology searches identified SLA dehydrogenase homologs in a range of putative sulfoglycolytic gene clusters in bacteria predominantly from the phyla Actinobacteria, Firmicutes, and Proteobacteria. This work provides a structural and biochemical view of SLA dehydrogenases to complement our knowledge of SLA reductases, and provide detailed insights into a critical step in the organosulfur cycle.
External linksChem Sci / PubMed:37886098 / PubMed Central
MethodsEM (single particle)
Resolution2.52 Å
Structure data

16433

8c54

EMDB-16433, PDB-8c54:
Cryo-EM structure of NADH bound SLA dehydrogenase RlGabD from Rhizobium leguminosarum bv. trifolii SRD1565
Method: EM (single particle) / Resolution: 2.52 Å

Chemicals

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE / Nicotinamide adenine dinucleotide

ChemComp-HOH:
WATER / Water

Source
  • rhizobium leguminosarum bv. trifolii srdi565 (bacteria)
KeywordsOXIDOREDUCTASE / Sulfolactaldehyde dehydrogenase NADH GabD

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