Evidence map›Paper›PMID 34752700›Full record

ArticleBiochemistry2021

Evidence for Proline Catabolic Enzymes in the Metabolism of Thiazolidine Carboxylates.

Yizi Mao, Javier Seravalli, Thomas G Smith, Martha Morton, John J Tanner, Donald F Becker

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 55% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. The Substrate Versatility of ΔMolecules (Basel, Switzerland) · 2026
    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 at 2 institutions in 1 country.

Yizi MaoDepartment of Biochemistry, Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588, United States.
Javier SeravalliDepartment of Biochemistry, Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588, United States.
Thomas G SmithDepartment of Chemistry, University of Nebraska, Lincoln, Nebraska 68588, United States.
Martha MortonDepartment of Chemistry, University of Nebraska, Lincoln, Nebraska 68588, United States.ORCID 0000-0002-6411-1733
John J TannerDepartments of Biochemistry and Chemistry, University of Missouri, Columbia, Missouri 65211, United States.ORCID 0000-0001-8314-113X
Donald F BeckerDepartment of Biochemistry, Redox Biology Center, University of Nebraska, Lincoln, Nebraska 68588, United States.ORCID 0000-0002-1350-7201
University of Nebraska–Lincoln · USUniversity of Missouri · US

Funding

Substrate Channeling and Communication in Proline Metabolic EnzymesR01GM065546 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI Donald F Becker, JOHN J TANNER · 2002 to 2026
$5.0M
NIGMS NIH HHS R01 GM065546
6 · The paper itself

Abstract

Thiazolidine carboxylates such as thiazolidine-4-carboxylate (T4C) and thiazolidine-2-carboxylate (T2C) are naturally occurring sulfur analogues of proline. These compounds have been observed to have both beneficial and toxic effects in cells. Given that proline dehydrogenase has been proposed to be a key enzyme in the oxidative metabolism of thioprolines, we characterized T4C and T2C as substrates of proline catabolic enzymes using proline utilization A (PutA), which is a bifunctional enzyme with proline dehydrogenase (PRODH) and l-glutamate-γ-semialdehyde dehydrogenase (GSALDH) activities. PutA is shown here to catalyze the FAD-dependent PRODH oxidation of both T4C and T2C with catalytic efficiencies significantly higher than with proline. Stopped-flow experiments also demonstrate that l-T4C and l-T2C reduce PutA-bound FAD at rates faster than proline. Unlike proline, however, oxidation of T4C and T2C does not generate a substrate for NAD

Indexed as

Bacterial ProteinsCysteineEnzyme AssaysKineticsMembrane ProteinsProlineRecombinant ProteinsSinorhizobium melilotiThiazolidinesBacterial ProteinsCysteineMembrane ProteinsProlinePutA protein, BacteriaRecombinant Proteinsthiazolidine-2-carboxylic acidthiazolidine-4-carboxylic acidThiazolidines

Identifiers

PMID34752700
PMCPMC8882339
OpenAlexW3211439764

What OpenQuestion holds

Textmetadata
LicenceTDM
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.