Evidence map›Paper›PMID 38878162›Full record

ArticleApplied biochemistry and biotechnology2024

Biochemical Characterization of a Marine Pseudoalteromonas citrea-Derived Fatty Acyl-AMP Ligase That Exhibits N-Acyl Amino Acid Synthetic Activity.

Keyan Li, Fuli Deng, Yonghua Wang, Fanghua Wang

Abstract read
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Article in Applied biochemistry and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Keyan Li *School of Food Science and Engineering, South China University of Technology, Guangzhou, 510640, People's Republic of China.
Fuli Deng *School of Food Science and Engineering, South China University of Technology, Guangzhou, 510640, People's Republic of China.
Yonghua WangSchool of Food Science and Engineering, South China University of Technology, Guangzhou, 510640, People's Republic of China.
Fanghua WangSchool of Food Science and Engineering, South China University of Technology, Guangzhou, 510640, People's Republic of China. wangfanghua@scut.edu.cn.

Funding

Basic and Applied Basic Research Foundation of Guangdong Province 2023A1515010859Key Research and Development Program of Guangdong Province 2022B0202010002National Key Research and Development Program of China 2022YFC2805101National Natural Science Foundation of China 31972014Science and Technology Planning Project of Guangdong Province 2022A0505050005Science and Technology Projects in Guangzhou 202201010757
6 · The paper itself

Abstract

Activation of fatty acids as acyl-adenylates by fatty acid-AMP ligase (FAAL) is a well-established process contributing to the formation of various functional natural products. Enzymatic characterization of FAALs is pivotal for unraveling both the catalytic mechanism and its role in specific biosynthetic pathways. In this study, we recombinantly expressed and characterized a novel FAAL derived from marine Pseudoalteromonas citrea (PcFAAL). PcFAAL was a cold-adapted neutral enzyme, demonstrating optimal activity at 30 °C and pH 7.5. Notably, its specific activity relied on the presence of Mg

Indexed as

PseudoalteromonasAmino AcidsBacterial ProteinsFatty AcidsHydrogen-Ion ConcentrationSubstrate SpecificityAmino AcidsBacterial ProteinsFatty AcidsATP-dependent amide bond synthesis activityEnzymatic characterizationFatty acyl-AMP ligasePseudoalteromonas citreaSubstrate specificity

Identifiers

PMID38878162

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.