Evidence map›Paper›PMID 10781553›Full record

ArticleJournal of bacteriology2000

Catabolism of alpha-ketoglutarate by a sucA mutant of Bradyrhizobium japonicum: evidence for an alternative tricarboxylic acid cycle.

L S Green, Y Li, D W Emerich, F J Bergersen, D A Day

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.5field-weighted citation impact, top 8% of its field
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

32 citing papers in PubMed, 79 citations in OpenAlex.

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  7. How Rhizobia Adapt to the Nodule Environment.Journal of bacteriology · 2021
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  8. Nitrogen Assimilation and Transport byInternational journal of molecular sciences · 2020
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  11. Review
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  14. Proteomic Characterization ofInternational journal of molecular sciences · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Biochemistry and evolution of anaerobic energy metabolism in eukaryotes.Microbiology and molecular biology reviews : MMBR · 2012
    Review
  20. 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

5 authors at 2 institutions in 2 countries.

L S GreenBiochemistry Department, University of Missouri, Columbia, Missouri 65211, USA. greenl@missouri.edu
Y Li
D W Emerich
F J Bergersen
D A Day
Australian National University · AUUniversity of Missouri · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A complete tricarboxylic acid (TCA) cycle is generally considered necessary for energy production from the dicarboxylic acid substrates malate, succinate, and fumarate. However, a Bradyrhizobium japonicum sucA mutant that is missing alpha-ketoglutarate dehydrogenase is able to grow on malate as its sole source of carbon. This mutant also fixes nitrogen in symbiosis with soybean, where dicarboxylic acids are its principal carbon substrate. Using a flow chamber system to make direct measurements of oxygen consumption and ammonium excretion, we confirmed that bacteroids formed by the sucA mutant displayed wild-type rates of respiration and nitrogen fixation. Despite the absence of alpha-ketoglutarate dehydrogenase activity, whole cells of the mutant were able to decarboxylate alpha-[U-(14)C]ketoglutarate and [U-(14)C]glutamate at rates similar to those of wild-type B. japonicum, indicating that there was an alternative route for alpha-ketoglutarate catabolism. Because cell extracts from B. japonicum decarboxylated [U-(14)C]glutamate very slowly, the gamma-aminobutyrate shunt is unlikely to be the pathway responsible for alpha-ketoglutarate catabolism in the mutant. In contrast, cell extracts from both the wild type and mutant showed a coenzyme A (CoA)-independent alpha-ketoglutarate decarboxylation activity. This activity was independent of pyridine nucleotides and was stimulated by thiamine PP(i). Thin-layer chromatography showed that the product of alpha-ketoglutarate decarboxylation was succinic semialdehyde. The CoA-independent alpha-ketoglutarate decarboxylase, along with succinate semialdehyde dehydrogenase, may form an alternative pathway for alpha-ketoglutarate catabolism, and this pathway may enhance TCA cycle function during symbiotic nitrogen fixation.

Indexed as

Citric Acid CycleAldehyde OxidoreductasesBradyrhizobiumCarboxy-LyasesDecarboxylationGene DeletionGlutamate DecarboxylaseGlutamic AcidKetoglutarate Dehydrogenase ComplexKetoglutaric AcidsMutagenesisNitrogen FixationSuccinate-Semialdehyde Dehydrogenase2-oxoglutarate decarboxylaseAldehyde OxidoreductasesCarboxy-LyasesGlutamate DecarboxylaseGlutamic AcidKetoglutarate Dehydrogenase ComplexKetoglutaric AcidsSuccinate-Semialdehyde Dehydrogenase

Identifiers

PMID10781553
PMCPMC101993
OpenAlexW2022561390

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.