AASDH

Last update 08 May 2025

Basic Info

Synonyms

AASDH, ACSF4, Acyl-CoA synthetase family member 4

+ [6]

Introduction

Covalently binds beta-alanine in an ATP-dependent manner to form a thioester bond with its phosphopantetheine group and transfers it to an, as yet, unknown acceptor. May be required for a post-translational protein modification or for post-transcriptional modification of an RNA.

100 Clinical Results associated with AASDH

100 Translational Medicine associated with AASDH

0 Patents (Medical) associated with AASDH

229

Literatures (Medical) associated with AASDH

08 Jan 2025·Journal of Agricultural and Food Chemistry

NRPS-like Gene LYS2 Contributed to the Biosynthesis of Cyclo(Pro-Val) in a Multistress-Tolerant Aromatic Probiotic, Meyerozyma guilliermondii GXDK6

Article

Author: Jiang, Chengjian ; Meng, Can ; He, Sheng ; Qin, Qiyu ; Bu, Ru ; Kashif, Muhammad ; Wei, Ruihang ; Chen, Xinglin ; Bai, Huashan ; Li, Zhenze ; Wu, Shanguang

Cyclo(Pro-Val) is a diketopiperazine (DKP) found widespread in marine microbes and resulting food products. With new bioactivities of cyclo(Pro-Val) being continually discovered, its potential applications in agriculture and food are becoming more evident, highlighting the need for efficient and practical methods to produce these compounds. However, the biosynthesis mechanisms of cyclo(Pro-Val), particularly in probiotics, remain unclear, and the functional identification of nonribosomal peptide synthases (NRPS) is still limited. This study presents a new efficient cyclo(Pro-Val) production system using the marine probiotic Meyerozyma guilliermondii (M. guilliermondii) GXDK6 as a chassis cell. We further characterized an NRPS-like gene, LYS2, which spans 3825 bp and encodes an l-2-amino-hexanedioic acid reductase (Lys2p) consisting of 1274 amino acids. A novel macrocyclization mechanism was revealed involving the peptide N-terminal and C-terminal imines mediated by Lys2p through nucleophilic reactions. Overexpressing LYS2 in GXDK6 resulted in a 45.5% increase in cyclo(Pro-Val) production, while knockout LYS2 completely halted its synthesis. This study revealed a novel metabolic regulatory pathway and biosynthetic mechanism for cyclo(Pro-Val) in marine yeast M. guilliermondii GXDK6. Refactoring the biosynthetic pathway in yeast through LYS2 provides an alternative approach for producing cyclo(Pro-Val).

01 Mar 2024·Biotechnology and Bioengineering

Demonstrating the immunostimulatory and cytokine‐augmentation effects of bacterial ghosts on natural killer cells and Caenorhabditis Elegans

Article

Author: Muhammad, Mumtaz ; Bhat, Sarita Ganapathy ; Narayanan, Sreeja ; Baburajan, Adheena Panangattu ; Joseph, Andrea ; Vemula, Praveen Kumar

AbstractThe potential of bacteria‐based immunotherapy lies in its ability to inherently enhance immune responses. However, the “liveness” of bacteria poses risks of bacterial escape, nonspecific immuno‐stimulation, and ethical concerns, limiting their acceptability in immunotherapy. In this scenario, nonliving empty bacterial‐cell envelopes, named bacterial ghosts (BGs), have emerged as immuno‐stimulants with the potential to side‐step the limitations of live bacterial therapies. This study demonstrates the capability of BGs in modulating the functionality of NK‐92 cells and Caenorhabditis elegans (C. elegans), as well as perform as cytokine‐therapy adjuvants. BGs were obtained through a pH‐driven culture method, and were validated for their structural and chemical integrity via electron microscopy and spectroscopy. In NK‐92 cells, BGs have shown significant immuno‐stimulation by boosting the gene‐expression of perforin, granzyme‐B, Fas‐L, and interferon‐gamma by factors of 3.5‐, 1.5‐, 12.5‐, and 8.6‐folds, respectively. Combined BG and IL‐12 treatment yielded a notable 10.2‐fold increase in interferon‐gamma protein expression in 24 h. The BGs also significantly influenced the innate immune response in C. elegans through the upregulation of lysozyme genes viz., ilys‐3 (8.8‐fold) and lys‐2 (3.1‐fold). Our investigation into the impact of BGs on natural killer cells and C. elegans highlights its potential as a valid alternative approach for new‐age immunotherapy and cytokine augmentation.

01 Feb 2024·International Immunopharmacology

Schisandrin A enhances pathogens resistance by targeting a conserved p38 MAPK pathway

Article

Author: Li, Sanhua ; Jiang, Nian ; Zhu, Xinting ; Liu, Liu ; Zhou, Hanlin ; Liu, Fang ; Cui, Yingwen ; Xiao, Yi ; Yu, Changyan

Schizandrin A (SA), also known as deoxyschizandrin, is one of the most biologically active lignans isolated from the traditional Chinese medicine Fructus schisandrae chinensis. Schisandrin A has proven benefits for anti-cancer, anti-inflammation, hepatoprotection, anti-oxidation, neuroprotection, anti-diabetes. But the influence of Schisandrin A to the innate immune response and its molecular mechanisms remain obscure. In this study, we found that Schisandrin A increased resistance to not only the Gram-negative pathogens Pseudomonas aeruginosa and Salmonella enterica but also the Gram-positive pathogen Listeria monocytogenes. Meanwhile, Schisandrin A protected the animals from the infection by enhancing the tolerance to the pathogens infection rather than by reducing the bacterial burden. Through the screening of the conserved immune pathways in Caenorhabditis elegans, we found that Schisandrin A enhanced innate immunity via p38 MAPK pathway. Furthermore, Schisandrin A increased the expression of antibacterial peptide genes, such as K08D8.5, lys-2, F35E12.5, T24B8.5, and C32H11.12 by activation PMK-1/p38 MAPK. Importantly, Schisandrin A-treated mice also enhanced resistance to P. aeruginosa PA14 infection and significantly increased the levels of active PMK-1. Thus, promoted PMK-1/p38 MAPK-mediated innate immunity by Schisandrin A is conserved from worms to mammals. Our work provides a conserved mechanism by which Schisandrin A enhances innate immune response and boosts its therapeutic application in the treatment of infectious diseases.

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AASDH

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