Evidence map›Paper›PMID 37071383›Full record

ArticleBiotechnology letters2023

Competitive inhibition of a non-natural cofactor dependent formaldehyde dehydrogenase by imidazole.

Junting Wang, Li Wan, Xiaojia Guo, Xueying Wang, Zongbao K Zhao

Abstract read
PubMed Publisher
In one paragraph

Article in Biotechnology letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 77% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

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

5 authors at 1 institution in 1 country.

Junting WangDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, China.
Li WanDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, China.
Xiaojia GuoDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, China.
Xueying WangDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, China. wangxueying@dicp.ac.cn.ORCID http://orcid.org/0000-0001-9291-793X
Zongbao K ZhaoDalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, 116023, China.
Dalian Institute of Chemical Physics · CN

Funding

Dalian Institute of Chemical Physics DICP I202020National Key R&D Program of China 2018YFA0900300National Natural Science Foundation of China 21907092National Natural Science Foundation of China 32001028
6 · The paper itself

Abstract

objectivesTo better understand the unique inhibitory behavior of a non-natural cofactor preferred formaldehyde dehydrogenase (FalDH) mutant 9B2.

resultsWe described our serendipitous observation that 9B2 was reversibly inhibited by residual imidazole introduced during protein preparation, while the wild-type enzyme was not sensitive to imidazole. Kinetic analysis showed that imidazole was a competitive inhibitor of formaldehyde with a K

conclusionThe mutant 9B2 can be competitively inhibited by imidazole, suggesting that cautions should be taken to evaluate activities as protein mutants might attain unexpected sensitivity to a component in buffers for purification or activity assays.

Indexed as

FormaldehydeImidazolesAldehyde OxidoreductasesKineticsMolecular Docking SimulationNiacinamideAldehyde OxidoreductasesFormaldehydeformaldehyde dehydrogenase, glutathione-independentImidazolesNiacinamideCompetitive inhibitionFormaldehyde dehydrogenaseImidazoleMutant enzyme

Identifiers

PMID37071383
OpenAlexW4366236439

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.