Mechanistic Insights into CYP199A4-Catalyzed α-Hydroxyketone Formation and Hydrogen Bond-Assisted C-C Bond Cleavage Catalyzed by the CYP199A4 F182L Mutant.

Chang Yuan, Jiaqi Xu, Shun Wang, Ye-Guang Fang, Hongwei Tan

Abstract read

In one paragraph

Article in International journal of molecular sciences, 2025. 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

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.

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.

Chang YuanInstitute of New Materials & Industrial Technologies, Wenzhou University, Wenzhou 325024, China.

Jiaqi XuKey Laboratories of Theoretical and Computational Photochemistry, Ministry of Education, Beijing Normal University, Beijing 100875, China.

Shun WangInstitute of New Materials & Industrial Technologies, Wenzhou University, Wenzhou 325024, China.

Ye-Guang FangInstitute of New Materials & Industrial Technologies, Wenzhou University, Wenzhou 325024, China.

Hongwei TanKey Laboratories of Theoretical and Computational Photochemistry, Ministry of Education, Beijing Normal University, Beijing 100875, China.ORCID 0000-0002-1376-6019

Funding

National Natural Science Foundation of China 22073010, 21571019, 21573020 and 21503018the Fundamental Research Funds for the Central Universities the Fundamental Research Funds for the Central Universitiesthe National Key Research and Development Program of China 2019YFC1805600

6 · The paper itself

Abstract

CYP199A4 is a cytochrome P450 and can catalyze the hydroxylation of 4-propionylbenzoic acid (4-pIBA) to generate α-hydroxyketone with high stereoselectivity. The F182L mutant of CYP199A4 (F182L-CYP199A4) has been shown to support the cleavage of the C-C bond between the carbonyl and hydroxyl groups of α-hydroxyketone, whereas wild-type CYP199A4 cannot. To uncover how the Phe182 regulates substrate reactivity, we conducted classical molecular dynamics (MD) and quantum mechanics/molecular mechanics (QM/MM) MD simulations on these systems. The results predicted that the formation of α-hydroxyketone preferentially led to the (

Indexed as

Cytochrome P-450 Enzyme SystemKetonesMutationCatalysisHydrogen BondingHydroxylationMolecular Dynamics SimulationCytochrome P-450 Enzyme SystemKetonesCYP199A4cytochrome P450 enzymeslyase reactionsprotein engineering

Identifiers

PMID40003992

DOI10.3390/ijms26041526

PMCPMC11854964

What OpenQuestion holds

Textmetadata

LicenceCC BY

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.