4’-Phosphopantetheine

4’-Phosphopantetheine is the prosthetic group of purified rat liver fatty acid synthetase, which accounts for over 90% of the bound label in the preparation^[1].
4′-Phosphopantetheine (100 μM; 48 h) increases intracellular 4′-phosphopantetheine levels in HoPan-treated Drosophila S2 cells, reversing the reduction caused by PANK inhibition^[2].
4′-Phosphopantetheine (25-800 μM; 48 h) rescues the reduced cell count phenotype in HoPan-treated Drosophila S2 cells in vitro in a concentration-dependent manner, with maximal rescue at 100-400 μM^[2].
4′-Phosphopantetheine (100 μM; 3 d) rescues the reduced cell count phenotype and histone acetylation in dPANK/fbl RNAi-treated Drosophila S2 cells^[2].
4′-Phosphopantetheine (25 μM; 4 d) rescues the reduced histone acetylation phenotype in HoPan-treated Drosophila S2 cells^[2].
4′-Phosphopantetheine (25 μM; 4 d) rescues the reduced cell count phenotype and intracellular CoA levels in HoPan-treated HEK293 cells^[2].
4′-Phosphopantetheine (100 μM; unspecified time) enters Drosophila S2 cells and is intracellularly converted to CoA, even under conditions of impaired de novo CoA biosynthesis caused by HoPan treatment^[2].
4′-Phosphopantetheine (100 μM; 10-30 min) enters Drosophila S2 cells via passive diffusion, as shown by temperature-independent uptake kinetics over 30 min of incubation with 100 μM labeled 4′-phosphopantetheine^[2].
4′-Phosphopantetheine (10-1000 μM; unspecified time) uptake by Drosophila S2 cells is concentration-dependent and temperature-independent, consistent with passive diffusion^[2].
4’-Phosphopantetheine (25-400 µM; 24 h) normalizes COASY gene expression in primary human PKAN fibroblasts in a dose-dependent manner^[3].
4'-Phosphopantetheine (0.23 μmoles; 30 min) isolated from hydrolyzed Escherichia coli ACP is enzymatically converted to CoA with 61% efficiency, confirming its identity as the prosthetic group of ACP^[4].
4'-Phosphopantetheine components in peptides isolated from peptic hydrolysates of ¹⁴C-malonyl-labeled Escherichia coli ACP are present in unimolar amounts, confirming 4'-Phosphopantetheine is the substrate-binding prosthetic group of ACP^[4].
4’-Phosphopantetheine (2.3-150 μM; 0, 10, 20, 30, 40 min) acts as a substrate for Staphylococcus aureus PPAT and exhibits significant substrate inhibition of the enzyme, while the cycloalkyl pyrimidine inhibitor competes with 4’-Phosphopantetheine for binding to the enzyme^[7].
4’-Phosphopantetheine (50-800 μM; 0, 10, 20, 30, 40 min) acts as a substrate for Streptococcus pneumoniae PPAT with a Michaelis constant of 223 μM, and the cycloalkyl pyrimidine inhibitor competes with 4’-Phosphopantetheine for binding to the enzyme and enzyme-ATP complex^[7].
4’-Phosphopantetheine (50 µM; 3 days, daily replenishment) normalizes complex I activity and reverses the glycolytic shift in primary human PKAN fibroblasts^[3].
4'-Phosphopantetheine (4 μM β-[³H]alanine; grown to late-logarithmic phase) accumulates as a major intracellular and extracellular metabolite in Escherichia coli strain SJ16^[5].
4'-Phosphopantetheine (4 μM β-[³H]alanine; up to 25 h of culture) is excreted into the growth medium of Escherichia coli strain SJ16 starting at 6 h of growth, accumulates continuously to 2.6 nmol/mL, and is not reutilized by the cells^[5].
4'-Phosphopantetheine (4 μM β-[³H]alanine, 4 μM β-[¹⁴C]alanine; overnight growth, grown to late-logarithmic phase) produced by Escherichia coli strain SJ16 originates from the degradation of intracellular ACP, rather than de novo biosynthesis from β-alanine^[5].
4'-Phosphopantetheine (0.8 μM, 0.6 μM; outgrowth assay, 1 h incubation at 37°C) cannot be assimilated by β-alanine-starved Escherichia coli strain SJ16 into CoA or ACP, nor used to support growth^[5].
4’-Phosphopantetheine (1 μg/mL; 24 h) inhibits ROS generation and ox-LDL accumulation in human umbilical vein vascular endothelial cells at a concentration of 1 μg/mL after 24 h of incubation^[8].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.