4.2.1.134: very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
This is an abbreviated version!
For detailed information about very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase, go to the full flat file.
Word Map on EC 4.2.1.134
-
4.2.1.134
-
elongase
-
vlcfas
-
myopathy
-
phosphatase-like
-
centronuclear
-
labrador
-
arrhythmogenic
-
biotechnology
- 4.2.1.134
- elongase
-
vlcfas
- myopathy
-
phosphatase-like
-
centronuclear
-
labrador
-
arrhythmogenic
- biotechnology
Reaction
Synonyms
3 hydroxyacyl-CoA dehydratase, 3-hydroxyacyl-CoA dehydratase, EC 2.3.1.119, Fatty acid elongase, fatty acyl-CoA dehydratase, HACD1, HACD2, HACD3, HACD4, HCD, PAS2, PASTICCINO 2, PASTICCINO2, PHS1, PTPLA, PTPLA dehydratase, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase, very-long-chain hydroxy fatty acyl-CoA dehydratase
ECTree
Advanced search results
General Information
General Information on EC 4.2.1.134 - very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
malfunction
metabolism
physiological function
-
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
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
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
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
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
malfunction
the hallmark of acylCoA dehydratase deficiency is the accumulation of the precursors, the 3-hydroxyacyl-CoAs
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
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
-
-
the enzyme catalyzes the third reaction of the four-step cycle in the elongation of very long-chain fatty acids
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
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
-
-
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
physiological function
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
physiological function
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
physiological function
PTPLA expression induces fatty acid elongation in yeast Tet-PHS1 in presence of DOX and in wild-type strain
physiological function
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
physiological function
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
physiological function
-
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
-
physiological function
-
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
-