Evidence map›Paper›PMID 39019246›Full record

ArticleBiochimica et biophysica acta. Proteins and proteomics2024

Kinetic characterization of the C-terminal domain of Malonyl-CoA reductase.

Mirela Tkalcic Cavuzic, Amanda Silva de Sousa, Jeremy R Lohman, Grover L Waldrop

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochimica et biophysica acta. Proteins and proteomics, 2024. 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
–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

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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.

  1. 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

4 authors.

Mirela Tkalcic CavuzicDepartment of Biological Sciences, Louisiana State University; Baton Rouge, LA 70803, USA. Electronic address: mtkalc1@lsu.edu.
Amanda Silva de SousaDepartment of Biochemistry and Molecular Biology, Michigan State University; East Lansing, MI 48824, USA. Electronic address: silvade3@msu.edu.
Jeremy R LohmanDepartment of Biochemistry and Molecular Biology, Michigan State University; East Lansing, MI 48824, USA. Electronic address: jlohman@msu.edu.
Grover L WaldropDepartment of Biological Sciences, Louisiana State University; Baton Rouge, LA 70803, USA. Electronic address: gwaldro@lsu.edu.

Funding

Malonyl-thioester Isosteres to Determine Enzyme Structure-Function Relationships - Undergrad SupplementR01GM140290 · NIGMS · PURDUE UNIVERSITY · PI LOHMAN, JEREMY RAY · 2020 to 2023
$1.2M
NIGMS NIH HHS R01 GM140290
6 · The paper itself

Abstract

Malonyl-CoA reductase utilizes two equivalents of NADPH to catalyze the reduction of malonyl-CoA to 3-hydroxypropionic acid (3HP). This reaction is part of the carbon fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus. The enzyme is composed of two domains. The C-terminal domain catalyzes the reduction of malonyl-CoA to malonic semialdehyde, while the N-terminal domain catalyzes the reduction of the aldehyde to 3HP. The two domains can be produced independently and retain their enzymatic activity. This report focuses on the kinetic characterization of the C-terminal domain. Initial velocity patterns and inhibition studies showed the kinetic mechanism is ordered with NADPH binding first followed by malonyl-CoA. Malonic semialdehyde is released first, while CoA and NADP

Indexed as

ChloroflexusMalonyl Coenzyme ANADPAlcohol OxidoreductasesBacterial ProteinsHydrogen-Ion ConcentrationKineticsLactic AcidOxidoreductasesProtein DomainsAlcohol OxidoreductasesBacterial Proteinshydracrylic acidLactic Acidmalonyl-Coa reductaseMalonyl Coenzyme ANADPOxidoreductasesAlcohol dehydrogenaseKinetic isotope effectsKinetic mechanismMalonyl-CoA reductaseShort-chain dehydrogenase/reductase

Identifiers

PMID39019246
PMCPMC12786355

What OpenQuestion holds

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Registered trials

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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.