This is the third component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long chain acyl CoAs. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase.
This is the third component of the elongase, a microsomal protein complex responsible for extending palmitoyl-CoA and stearoyl-CoA (and modified forms thereof) to very-long chain acyl CoAs. cf. EC 2.3.1.199, very-long-chain 3-oxoacyl-CoA synthase, EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase.
enzyme expression analysis, pPAS2:GUS staining is present in mature roots and secondary roots but also expressed in the epidermis of cotyledons and leaves. In mature primary roots, pPAS2:GUS expression profile is specific to the endodermis
enzyme expression analysis, pPAS2:GUS staining is present in mature roots and secondary roots but also expressed in the epidermis of cotyledons and leaves. In mature primary roots, pPAS2:GUS expression profile is specific to the endodermis
enzyme expression analysis, pPTPLA:GUS staining is specifically localized in mature primary and secondary roots and restricted to the central cylinder. In mature primary roots pPTPLA:GUS appears to be restricted to vascular tissue
enzyme expression analysis, pPTPLA:GUS staining is specifically localized in mature primary and secondary roots and restricted to the central cylinder. In mature primary roots pPTPLA:GUS appears to be restricted to vascular tissue
the very-long-chain 3-hydroxyacyl-CoA dehydratase PTPLA sequence is as divergent from very-long-chain 3-hydroxyacyl-CoA dehydratase PAS2 sequence as it is from yeast very-long-chain 3-hydroxyacyl-CoA dehydratase PHS1
complete loss of enzyme function is embryo lethal. The pas2-1 mutant is characterized by a general reduction of very-long-chain fatty acid pools in seed storage triacylglycerols, cuticular waxes, and complex sphingolipids
mutation in the pas2 gene causes a reduction of very-long-chain fatty acids levels that lead to specific accumulation of cells in late mitosis with delayed, unfinished or abnormal cell plates
reduced enzyme levels result in significant impairment of the conversion of ceramide to inositol phosphorylceramide, cause an accumulation of ceramide and a reduction in complex sphingolipids
an enzyme mutant strain exhibits sensitivity to cell wall stress agents and loss of shooting due to a delay in ballistospore formation. The phs1 deletion mutation in Sporobolomyces causes reduction in 3-hydroxyacyl-CoA dehydratase activity and alters the lipid profiles of the cells, mirror mutant phenotype, overview. Stress phenotypes of the phs1 mutant of Sporobolomyces suggest that defects in other cellular processes can impair the formation of spores, overview
loss of function of the elongase 3 hydroxyacyl-CoA dehydratase PHS1 in yeast prevents growth and induces cytokinesis defects. Protein tyrosine phosphatase-like (PTPLA) is able to restore yeast phs1 growth and very long chain fatty acids (VLCFAs) elongation, phenotype of the PTPLA complementation of Tet-PHS1 mutant. The absence of the dehydratase PHS1 blocks fatty acid elongation and leads to reduced VLCFA levels in yeast. As a corollary, phytosphingosine (PHS) level is enhanced since VLCFA are required for sphingolipids synthesis. PTPLA expression in Tet-PHS1+DOX is able to reduce PHS levels and induce VLCFA elongation to wild-type levels. The hallmark of acylCoA dehydratase deficiency is the accumulation of the precursors, the 3-hydroxyacyl-CoAs
the hallmark of acylCoA dehydratase deficiency is the accumulation of the precursors, the 3-hydroxyacyl-CoAs. Loss of function of the elongase 3 hydroxyacyl-CoA dehydratase PASTICCINO2 (pas2-1) in plants prevents growth and induces cytokinesis defects. The disruption of VLCFA elongation in pas2-1 mutant induces cell proliferation and abnormal cytokinesis leading to defective differentiation in the apical part and shorter primary root. These developmental defects were linked with reduced VLCFA levels in triglycerides, waxes, sphingolipids and phospholipids. Moreover, the complete loss of PAS2 function is embryo lethal. Protein tyrosine phosphatase-like (PTPLA) is not able to restore the plant pas2-1 defects. The lack of complementation of a null allele of yeast phs1 could be caused by some plant specific determinants of PTPLA activity
an enzyme mutant strain exhibits sensitivity to cell wall stress agents and loss of shooting due to a delay in ballistospore formation. The phs1 deletion mutation in Sporobolomyces causes reduction in 3-hydroxyacyl-CoA dehydratase activity and alters the lipid profiles of the cells, mirror mutant phenotype, overview. Stress phenotypes of the phs1 mutant of Sporobolomyces suggest that defects in other cellular processes can impair the formation of spores, overview
the enzyme is involved in the fatty acid synthesis, pathway overview. De novo assembly and functional annotation of Aurantiochytrium transcriptome and library screening to determinthe enzymes important for docosahexenoic acid biosynthesis, overview
the enzyme is involved in the fatty acid synthesis, pathway overview. De novo assembly and functional annotation of Aurantiochytrium transcriptome and library screening to determinthe enzymes important for docosahexenoic acid biosynthesis, overview
the enzyme is essential and limiting for Arabidopsis development. Enzyme-derived very-long-chain fatty acid homeostasis is required for specific developmental processes. The enzyme is involved in 3-hydroxy acyl-coa dehydration during very-long-chain fatty acid elongation
comparative ectopic expression of the two very-long-chain 3-hydroxyacyl-CoA dehydratases PTPLA and PAS2 in their respective domains confirms the existence of two independent elongase complexes based on PAS2 or PTPLA dehydratase that are functionally interacting. The two dehydratases have specific expression profiles in the root with PAS2 mostly restricted to the endodermis, while PTPLA is confined in the vascular tissue and pericycle cells
comparative ectopic expression of the two very-long-chain 3-hydroxyacyl-CoA dehydratases PTPLA and PAS2 in their respective domains confirms the existence of two independent elongase complexes based on PAS2 or PTPLA dehydratase that are functionally interacting. The two dehydratases have specific expression profiles in the root with PAS2 mostly restricted to the endodermis, while PTPLA is confined in the vascular tissue and pericycle cells. Protein tyrosine phosphatase-like (PTPLA), previously characterized as an inactive dehydratase, is not able to restore the plant pas2-1 defects. Enzyme PTPLA associates with the elongase complex in the endoplasmic reticulum. The specific elongase activity in vascular tissues regulates endodermal VLCFA elongation
the 3-hydroxyacyl-CoA dehydratase is required for the third step in very long chain fatty acid biosynthesis. The role of Phs1 in spore dissemination may be primarily in cellular integrity
the enzyme is involved in fatty acid synthesis. The very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase catalyzes fatty acid elongation from C20:5 to C22:5. The enzyme activity is correlated to the docosahexenoic acid (DHA) content, reduction of enzyme expression leads to reduced DHA
the enzyme is involved in fatty acid synthesis. The very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase catalyzes fatty acid elongation from C20:5 to C22:5. The enzyme activity is correlated to the docosahexenoic acid (DHA) content, reduction of enzyme expression leads to reduced DHA
the 3-hydroxyacyl-CoA dehydratase is required for the third step in very long chain fatty acid biosynthesis. The role of Phs1 in spore dissemination may be primarily in cellular integrity
construction of a Sporobolomyces phs1 mutant strain GI209 by T-DNA insertion. The mutant has less dehydratase activity and a reduction in very long chain fatty acids compared to wild-type. The phs1 mutation in Sporobolomyces causes reduction in 3-hydroxyacyl-CoA dehydratase activity and alters the lipid profiles of the cells. The mutant strain also exhibits sensitivity to cell wall stress agents and loss of shooting due to a delay in ballistospore formation
construction of a Sporobolomyces phs1 mutant strain GI209 by T-DNA insertion. The mutant has less dehydratase activity and a reduction in very long chain fatty acids compared to wild-type. The phs1 mutation in Sporobolomyces causes reduction in 3-hydroxyacyl-CoA dehydratase activity and alters the lipid profiles of the cells. The mutant strain also exhibits sensitivity to cell wall stress agents and loss of shooting due to a delay in ballistospore formation
gene MTH12.2 or At5g59770, expression analysis, PTPLA is fused with CYFP- or NYFP- at the N-terminal of the protein prevent potential interference with ER retention signal located at the C-terminal end, transient expression of 35S:mCherry-PTPLA constructs in Nicotiana benthamiana. The subcellular distribution of mCherry-PTPLA shows the characteristic endoplasmic reticulum network which is confirmed by its colocalization with endoplasmic reticulum-localized GFP-PAS2 fusion, in contrary to the PTPLA promoter, the KCR2 promoter is also expressed in cotyledons, leaves and in the meristem of secondary roots
gene phs1, encoding 3-hydroxyacyl-CoA dehydratase required for the third step in very long chain fatty acid biosynthesis, the Sporobolomyces sp. PHS1 gene complements the essential functions of the Saccharomyces cerevisiae phs1 loss-of-function mutant strain phs1::KanMX/PHS1, transfection using the Agrobacterium tumefaciens system, lipid analysis of the strains
the enzyme is a potential target for biotechnological optimization of the production of docosahexenoic acid (DHA) in the Aurantiochytrium sp. thraustochytrid strain PKUSW7
the enzyme is a potential target for biotechnological optimization of the production of docosahexenoic acid (DHA) in the Aurantiochytrium sp. thraustochytrid strain PKUSW7
Transcriptomic profiling and gene disruption revealed that two genes related to Pufas/DHA biosynthesis may be essential for cell growth of Aurantiochytrium sp.