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ReviewMedicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents2026

FabH (β-Ketoacyl-ACP Synthase III) -- Promising Novel Antibacterial Target and Its Inhibitors.

Gui-Wen Li, Qing-Yun Rong, Wen Zhang, Guo-Wu Rao, Quan Zheng

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In one paragraph

Review in Medicinal chemistry research : an international journal for rapid communications on design and mechanisms of action of biologically active agents, 2026. 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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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

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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Gui-Wen LiCollege of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, P. R. China.
Qing-Yun RongCollege of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, P. R. China.
Wen ZhangCollege of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, P. R. China.
Guo-Wu RaoCollege of Pharmaceutical Science, Zhejiang University of Technology, Hangzhou, P. R. China. rgw@zjut.edu.cn.
Quan ZhengDepartment of Medical Oncology, The Quzhou Affiliated Hospital of Wenzhou Medical University, Quzhou People's Hospital, Quzhou, P. R. China. zhengquan@wmu.edu.cn.

Funding

Natural Science Foundation of Zhejiang Province LY19B020008the National Natural Science Foundation of China 21877101the Science and Technology Program of Zhejiang Province 2018R01015
6 · The paper itself

Abstract

The worldwide spread of antimicrobial resistance (AMR) is a considerable challenge to global health, resulting in a substantial depletion of human and material resources. Conventional antimicrobial agents are often ineffective against contemporary resistant strains, making the identification of novel drug targets a priority in antimicrobial development. Inhibition of the bacterial type II fatty acid synthesis (FAS-II) pathway is recognized as an effective antimicrobial strategy. β-Ketoacyl-ACP synthase III (FabH), a crucial enzyme in the FAS-II, presents potential as a target for next-generation antimicrobial agents. In recent years (2006-2025), research on synthetic small-molecule inhibitors targeting FabH has attracted widespread attention among scientists. However, reviews on FabH inhibitors remain scarce, with reports scattered across the literature. This paper outlines the attributes of FabH in various bacterial species and compiles the currently documented synthetic inhibitors. It examines the inhibitory effects of various core structures on FabH and analyzes the structure-activity relationships of specific compounds, including triazoles, carbazoles, indoles, and pyrazoles, etc. The goal is to offer innovative perspectives for the future development and formulation of antibacterial agents targeting FabH.

Indexed as

3-Oxoacyl-(Acyl-Carrier-Protein) SynthaseAnti-Bacterial AgentsBacteriaEnzyme InhibitorsHumansStructure-Activity Relationship3-ketoacyl-acyl carrier protein synthase III3-Oxoacyl-(Acyl-Carrier-Protein) SynthaseAnti-Bacterial AgentsEnzyme InhibitorsAntimicrobial resistanceFAS-IIMultidrug-resistant bacteriaStructure-activity relationshipsSynthetic small-molecule inhibitors

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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.