Evidence map›Paper›PMID 39840830›Full record

ArticleThe Biochemical journal2025

Structure, kinetics, and mechanism of Pseudomonas putida sulfoquinovose dehydrogenase, the first enzyme in the sulfoglycolytic Entner-Doudoroff pathway.

Laura Burchill, Mahima Sharma, Niccolay Madiedo Soler, Ethan D Goddard-Borger, Gideon J Davies, Spencer J Williams

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Biochemical journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Review
  2. Advances in microbial sulfoquinovose catabolism.Frontiers in microbiology · 2026
    Review
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Laura BurchillSchool of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria 3010, Australia.
Mahima SharmaDepartment of Chemistry, York Structural Biology Laboratory, University of York, York YO10 5DD, U.K.
Niccolay Madiedo SolerThe Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, 3052, Australia.
Ethan D Goddard-BorgerThe Walter and Eliza Hall Institute of Medical Research, Parkville, Victoria, 3052, Australia.
Gideon J DaviesDepartment of Chemistry, York Structural Biology Laboratory, University of York, York YO10 5DD, U.K.
Spencer J WilliamsSchool of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Victoria 3010, Australia.ORCID 0000-0001-6341-4364

Funding

Biotechnology and Biological Sciences Research Council BB/W003805/1
6 · The paper itself

Abstract

The sulfosugar sulfoquinovose (SQ) is catabolized through the sulfoglycolytic Entner-Doudoroff pathway, beginning with the oxidation of SQ to sulfogluconolactone by SQ dehydrogenase. We present a comprehensive structural and kinetic characterization of Pseudomonas putida SQ dehydrogenase (PpSQDH). PpSQDH is a tetrameric enzyme belonging to the short-chain dehydrogenase/reductase (SDR) superfamily with a strong preference for NAD+ over NADP+. Kinetic analysis revealed a rapid equilibrium ordered mechanism in which the NAD+ cofactor is the first substrate to bind, and NADH is the last product to dissociate. Structural studies revealed a homotetrameric structure in solution and crystals, involving cross-subunit interactions in which the C-terminus residue (Gln260) inserts into the diagonally opposite subunit to form part of the second shell of residues lining the active site. Complexes of PpSQDH with SQ or NAD+ provide insight into the recognition of SQ and together with the kinetic analysis allow the proposal of a catalytic reaction mechanism. Our findings illuminate the mechanism of SQ degradation and the evolution of the SDR superfamily for organosulfonate catabolism.

Indexed as

Bacterial ProteinsPseudomonas putidaCatalytic DomainCrystallography, X-RayKineticsModels, MolecularNADNADPSubstrate SpecificityBacterial ProteinsNADNADPenzyme mechanismorganosulfurshort-chain dehydrogenase/reductasesulfoglycolysissulfur cycle

Identifiers

PMID39840830
PMCPMC12133307

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.