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Last update 23 Jan 2025

OXSM

Last update 23 Jan 2025

Basic Info

Synonyms

3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial, 3-oxoacyl-ACP synthase, mitochondrial, Beta-ketoacyl-ACP synthase

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Introduction

May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function.

Drugs associated with OXSM

Platensimycin

Target

OXSM

Mechanism

OXSM inhibitors

Active Org.

Merck & Co., Inc.

Originator Org.

Merck & Co., Inc.

Active Indication

Antibiotic resistant infection

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

JSF-3285

Target

OXSM

Mechanism

OXSM inhibitors

Active Org.

Rutgers State University of New Jersey

Originator Org.

Rutgers State University of New Jersey

Active Indication

Tuberculosis

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Platencin

Target

OXSM

Mechanism

OXSM inhibitors

Active Org.

Merck Research Laboratories Massachusetts LLC

Originator Org.

Merck Research Laboratories Massachusetts LLC

Active Indication

Bacterial Infections

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with OXSM

100 Translational Medicine associated with OXSM

0 Patents (Medical) associated with OXSM

406

Literatures (Medical) associated with OXSM

01 Jan 2025·Theoretical and Applied Genetics

A β-ketoacyl-CoA synthase encoded by DDP1 controls rice anther dehiscence and pollen fertility by maintaining lipid homeostasis in the tapetum

Article

Author: Wei, Jianxin ; Xu, Yibo ; He, Xinhua ; Shang, Lianguang ; Zhao, Wenfeng ; He, Juan ; Wang, Yongfei ; Zhou, Shixu ; Qin, Baoxiang ; Tian, Jingfei ; Tan, Wenye ; Li, Rongbai

KEY MESSAGEDDP1, encoding a β-Ketoacyl-CoA Synthase, regulates rice anther dehiscence and pollen fertility by affecting the deposition of lipid on anther epidermis and pollen wall. Anther dehiscence and pollen fertility are crucial for male fertility in rice. Here, we studied the function of Defective in Dehiscence and Pollen1 (DDP1), a novel member of the KCS family in rice, in regulating anther dehiscence and pollen fertility. DDP1 encodes an endoplasmic reticulum (ER)-localized protein and is ubiquitously expressed in various organs, predominately in the microspores and tapetum. The ddp1 mutant exhibited partial male sterility attributed to defective anther dehiscence and pollen fertility, which was notably distinct from those observed in Arabidopsis thaliana and rice mutants associated with lipid metabolism. Mutations of DDP1 altered the content and composition of wax on anther epidermis and pollen wall, causing abnormalities in their morphology. Moreover, genes implicated in lipid metabolism, pollen development, and anther dehiscence exhibited significantly altered expression levels in the ddp1 mutant. These findings indicate that DDP1 controls anther dehiscence and pollen fertility to ensure normal male development by modulating lipid homeostasis in the tapetum, thereby enhancing our understanding of the mechanisms underlying rice anther dehiscence and pollen fertility.

30 Oct 2024·Journal of the American Chemical Society

Hybrid Type I and II Polyketide Synthases Yield Distinct Aromatic Polyketides

Article

Author: Shi, Jing ; Sun, Jia Lin ; Yan, Zhang Yuan ; Xu, Zhao Yang ; Jiao, Rui Hua ; Tan, Ren Xiang ; Tong, Zhi Wu ; Zhao, Li Ya ; Ge, Hui Ming

Bacterial aromatic polyketides are compounds with multiple aromatic rings synthesized by bacterial type II polyketide synthases (PKSs), some of which have been developed into clinical drugs. Compounds containing aromatic polyketides synthesized by hybrid type I and type II PKSs are extremely rare. Here, we report the discovery of a gene cluster encoding both modular type I and type II PKSs as well as KAS III through extensive bioinformatics analysis, leading to the characterization of the hybrid polyketide, spirocycline A. The structure of spirocycline A is rare among all aromatic polyketides, featuring a unique starter unit and four spirocycles and forming a dimer. Biosynthetic studies indicate that the starter unit of this molecule is synthesized by type I PKS in collaboration with two trans-acting ketoreductase (KR) and enoylreductase (ER). It is then transferred by KAS III to the type II PKS system, which synthesizes the tricyclic aromatic polyketide backbone. The subsequent formation of the spirocycle and dimerization are carried out by four redox enzymes encoded in the gene cluster. Overall, the discovery of spirocycline A provides a new approach for identifying novel aromatic polyketides and offers potential enzymatic tools for the bioengineering of these hybrid polyketides.

01 Oct 2024·Archives of Microbiology

Screening of promising molecules against potential drug targets in Yersinia pestis by integrative pan and subtractive genomics, docking and simulation approach

Article

Author: Li, Yanping ; Kumar, Suresh ; Chen, Lei ; Qiao, Liang ; Zhang, Lihu

This study focuses on Yersinia pestis, the bacterium responsible for plague, which posed a severe threat to public health in history. Despite the availability of antibiotics treatment, the emergence of antibiotic resistance in this pathogen has increased challenges of controlling the infections and plague outbreaks. The development of new drug targets and therapies is urgently needed. This research aims to identify novel protein targets from 28 Y. pestis strains by the integrative pan-genomic and subtractive genomics approach. Additionally, it seeks to screen out potential safe and effective alternative therapies against these targets via high-throughput virtual screening. Targets should lack homology to human, gut microbiota, and known human 'anti-targets', while should exhibit essentiality for pathogen's survival and virulence, druggability, antibiotic resistance, and broad spectrum across multiple pathogenic bacteria. We identified two promising targets: the aminotransferase class I/class II domain-containing protein and 3-oxoacyl-[acyl-carrier-protein] synthase 2. These proteins were modeled using AlphaFold2, validated through several structural analyses, and were subjected to molecular docking and ADMET analysis. Molecular dynamics simulations determined the stability of the ligand-target complexes, providing potential therapeutic options against Y. pestis.

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