EC Number   |
General Information |
Reference |
|---|
    4.2.1.134 | evolution |
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 |
749092 |
| 4.2.1.134 | malfunction |
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 |
-, 749134 |
| 4.2.1.134 | malfunction |
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 |
720893 |
| 4.2.1.134 | malfunction |
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 |
749092 |
| 4.2.1.134 | malfunction |
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 |
720091 |
| 4.2.1.134 | malfunction |
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 |
719847 |
| 4.2.1.134 | malfunction |
the hallmark of acylCoA dehydratase deficiency is the accumulation of the precursors, the 3-hydroxyacyl-CoAs |
749092 |
| 4.2.1.134 | malfunction |
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 |
749092 |
| 4.2.1.134 | metabolism |
the enzyme catalyzes the third reaction of the four-step cycle in the elongation of very long-chain fatty acids |
719847 |
| 4.2.1.134 | metabolism |
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 |
-, 748533 |
