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
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4.2.1.134
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elongase
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vlcfas
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myopathy
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phosphatase-like
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centronuclear
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labrador
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arrhythmogenic
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biotechnology
- 4.2.1.134
- elongase
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vlcfas
- myopathy
-
phosphatase-like
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centronuclear
-
labrador
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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
4.2.1.134 very-long-chain (3R)-3-hydroxyacyl-CoA dehydrataseAdvanced search results
results (
results (Engineering
Engineering on EC 4.2.1.134 - very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E116A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
E156A
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inactive, the mutant cannot suppress phytosphingosine accumulation, although the protein is expressed normally
E60A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
F145A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
G152A
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mutant with reduced activity, the mutant cannot suppress phytosphingosine accumulation, although the protein is expressed normally
L12A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
N16A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
P150A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
P188A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
Q200A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
Q54A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
Q79A
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inactive, the mutant cannot suppress phytosphingosine accumulation, although the protein is expressed normally
R119A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
R141A
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mutant with reduced activity, the mutant cannot suppress phytosphingosine accumulation, although the protein is expressed normally
R201A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
R83A
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mutant with reduced activity, the mutant cannot suppress phytosphingosine accumulation, although the protein is expressed normally
W124A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
W23A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
Y142A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
Y149A
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inactive, the mutant cannot suppress phytosphingosine accumulation, although the protein is expressed normally
Y15A
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phytosphingosine accumulates at low levels in the mutant compared with wild type cells
additional information
additional information
construction of an enzyme deletion mutant DELTAPH, phenotype, overview
additional information
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construction of an enzyme deletion mutant DELTAPH, phenotype, overview
additional information
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construction of an enzyme deletion mutant DELTAPH, phenotype, overview
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additional information
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
additional information
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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
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