Ask about this productRelated genes to: PPAT antibody
- Gene:
- COASY NIH gene
- Name:
- Coenzyme A synthase
- Previous symbol:
- -
- Synonyms:
- DPCK, NBP, CoASY, PPAT
- Chromosome:
- 17q21.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-22
- Date modifiied:
- 2015-11-11
- Gene:
- PPAT NIH gene
- Name:
- phosphoribosyl pyrophosphate amidotransferase
- Previous symbol:
- -
- Synonyms:
- GPAT, PRAT
- Chromosome:
- 4q12
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2015-08-25
Related products to: PPAT antibody
Related articles to: PPAT antibody
- sp. ATCC 20888 is an important species for industrial polyunsaturated fatty acids (PUFA) production. This study investigated the regulatory mechanisms affecting the proportions of eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA) in terms of biosynthesis and storage distribution. EPA and DHA possessed different accumulation patterns: EPA proportion increased over time, while DHA peaked at 48 h. EPA was predominantly integrated into triacylglycerol during the logarithmic phase and phosphatidylcholine during the stationary phase. Transcriptome analysis revealed that EPA synthesis involved the fatty acid synthase-elongase/desaturase system, while DHA depended mainly on PUFA synthase. Key enzymes, including elongase ELOVL7, diacylglycerol acyltransferase (g10562), and lysophosphatidylcholine acyltransferases (g8836 and g7540), show a positive correlation with EPA yield, highlighting their roles in its biosynthesis and storage. Additionally, phosphopantetheine adenylyl transferase (PPAT/COASY) and ADP-ribosylation factor 1_2 (ARF1_2) were identified as potential regulators of PUFA proportions. This study provided insights for genetic optimization of PUFA production in. - Source: PubMed
Publication date: 2025/02/05
Xu YaqiZhang ZhaoBian YanqingWang YuanhaoDeng ZiliangLuo RuiLi WeijiaYan JingyiZhao BaohuaSun Dongzhe - CoA Synthase (CoASy, 4'-phosphopantetheine adenylyltransferase/dephospho-CoA kinase) mediates two final stages of de novo coenzyme A (CoA) biosynthesis in higher eukaryotes. Unfortunately very little is known about regulation of this important metabolic pathway. In this study, we demonstrate that CoASy interacts in vitro with Src homology-2 (SH2) domains of a number of signaling proteins, including Src homology-2 domains containing protein tyrosine phosphatase (Shp2PTP). Complexes between CoASy and Shp2PTP exist in vivo in mammalian cells and this interaction is regulated in a growth-factor-dependent manner. We have also demonstrated that endogenous CoASy is phosphorylated on tyrosine residues in vivo, and that cytoplasmic protein tyrosine kinases can mediate this phosphorylation in vitro and in vivo. Importantly, Shp2PTP-mediated CoASy in vitro dephosphorylation leads to an increase in CoASy enzymatic phosphopantetheine adenylyltransferase (PPAT) activity. We therefore argue that CoASy is a novel potential substrate of Shp2PTP and phosphorylation of CoASy at tyrosine residue(s) could represent unrecognized before mechanism of modulation intracellular CoA level in response to hormonal and (or) other extracellular stimuli. - Source: PubMed
Publication date: 2009/09/18
Breus OksanaPanasyuk GannaGout Ivan TFilonenko ValeriyNemazanyy Ivan