Evidence map›Paper›PMID 17954980›Full record

ReviewJournal of biosciences2007

Structure and function of enzymes involved in the anaerobic degradation of L-threonine to propionate.

Dhirendra K Simanshu, Sagar Chittori, H S Savithri, M R N Murthy

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of biosciences, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

12 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Hazelnut: Explorations toward the Biocatalytic Synthesis of its Aroma Precursor.Chembiochem : a European journal of chemical biology · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Mutation accumulation and horizontal gene transfer inCommunicative & integrative biology · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Article
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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

4 authors at 1 institution in 1 country.

Dhirendra K SimanshuMolecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, India.
Sagar Chittori
H S Savithri
M R N Murthy
Indian Institute of Science Bangalore · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In Escherichia coli and Salmonella typhimurium, L-threonine is cleaved non-oxidatively to propionate via 2-ketobutyrate by biodegradative threonine deaminase, 2-ketobutyrate formate-lyase (or pyruvate formate-lyase), phosphotransacetylase and propionate kinase. In the anaerobic condition, L-threonine is converted to the energy-rich keto acid and this is subsequently catabolised to produce ATP via substrate-level phosphorylation, providing a source of energy to the cells. Most of the enzymes involved in the degradation of L-threonine to propionate are encoded by the anaerobically regulated tdc operon. In the recent past, extensive structural and biochemical studies have been carried out on these enzymes by various groups. Besides detailed structural and functional insights, these studies have also shown the similarities and differences between the other related enzymes present in the metabolic network. In this paper, we review the structural and biochemical studies carried out on these enzymes.

Indexed as

AnaerobiosisBacterial ProteinsBiotransformationEnzymesPropionatesStructure-Activity RelationshipThreonineBacterial ProteinsEnzymesPropionatespropionic acidThreonine

Identifiers

PMID17954980
OpenAlexW2085913418

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.