Information on EC 4.2.1.134 - very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
4.2.1.134
-
RECOMMENDED NAME
GeneOntology No.
very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] = a very-long-chain trans-2,3-dehydroacyl-[acyl-carrier protein] + H2O
show the reaction diagram
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
Biosynthesis of unsaturated fatty acids
-
Fatty acid elongation
-
very long chain fatty acid biosynthesis I
-
very long chain fatty acid biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] hydro-lyase
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3-hydroxyacyl-CoA dehydratase
Q8VZB2
-
3-hydroxyacyl-CoA dehydratase
-
-
3-hydroxyacyl-CoA dehydratase
-
-
fatty acyl-CoA dehydratase
-
-
HACD1
-
isoform
HACD2
-
isoform
HACD3
-
isoform
HACD4
-
isoform
PAS2
-
-
gene name
-
PAS2
Q8VZB2
PASTICCINO 2, gene name
PASTICCINO2
-
gene name
PHS1
-
-
gene name
-
very-long-chain hydroxy fatty acyl-CoA dehydratase
-
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ecotype Col-0
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
-, Q8VZB2
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
-
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
metabolism
-
the enzyme catalyzes the third reaction of the four-step cycle in the elongation of very long-chain fatty acids
physiological function
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
3-hydroxyacyl-CoA
2,3-trans-enoyl-CoA + H2O
show the reaction diagram
-
-
-
-
?
3-hydroxyacyl-CoA
2,3-trans-enoyl-CoA + H2O
show the reaction diagram
-
-
-
-
?
3-hydroxyacyl-CoA
enoyl-CoA + H2O
show the reaction diagram
-, Q8VZB2
-
-
-
?
3-hydroxypalmitoyl-CoA
2,3-trans-hexadecenoyl-CoA + H2O
show the reaction diagram
-
-
-
-
?
3-hydroxypalmitoyl-CoA
2,3-trans-hexadecenoyl-CoA + H2O
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-hydroxyacyl-CoA
2,3-trans-enoyl-CoA + H2O
show the reaction diagram
-
-
-
-
?
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
flufenacet
-, Q8VZB2
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0068
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3-hydroxypalmitoyl-CoA
-
isoform HCAD4, in 50 mM HEPES-NaOH (pH 7.4), 150 mM NaCl, 10% (v/v) glycerol, 1 mM dithiothreitol, 1 mM phenylmethylsulfonyl fluoride, at 37C
0.0336
-
3-hydroxypalmitoyl-CoA
-
isoform HCAD1, in 50 mM HEPES-NaOH (pH 7.4), 150 mM NaCl, 10% (v/v) glycerol, 1 mM dithiothreitol, 1 mM phenylmethylsulfonyl fluoride, at 37C
0.0495
-
3-hydroxypalmitoyl-CoA
-
isoform HCAD3, in 50 mM HEPES-NaOH (pH 7.4), 150 mM NaCl, 10% (v/v) glycerol, 1 mM dithiothreitol, 1 mM phenylmethylsulfonyl fluoride, at 37C
0.1217
-
3-hydroxypalmitoyl-CoA
-
isoform HCAD2, in 50 mM HEPES-NaOH (pH 7.4), 150 mM NaCl, 10% (v/v) glycerol, 1 mM dithiothreitol, 1 mM phenylmethylsulfonyl fluoride, at 37C
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is specifically associated in the endoplasmic reticulum with the enoyl-CoA reductase CER10
Manually annotated by BRENDA team
-
a membranespanning protein that traverses the membrane six times and has an N-terminus and C-terminus facing the cytosol
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 54900, EGFP-tagged HACD4 isoform, estimated from amino acid sequence; x * 55800, EGFP-tagged HACD2 isoform, estimated from amino acid sequence; x * 59800, EGFP-tagged HACD1 isoform, estimated from amino acid sequence; x * 70600, EGFP-tagged HACD3 isoform, estimated from amino acid sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Nicotiana benthamiana and Arabidopsis thaliana epidermal cells
-
expressed in Saccharomyces cerevisiae strain SAY32
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ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E116A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells
E156A
-
inactive, the mutant cannot suppress phytosphingosine accumulation, although the protein is expressed normally
E60A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells
F145A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells
G152A
-
mutant with reduced activity, the mutant cannot suppress phytosphingosine accumulation, although the protein is expressed normally
L12A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells
N16A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells
P150A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells
P188A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells
Q200A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells
Q54A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells
Q79A
-
inactive, the mutant cannot suppress phytosphingosine accumulation, although the protein is expressed normally
R119A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells
R141A
-
mutant with reduced activity, the mutant cannot suppress phytosphingosine accumulation, although the protein is expressed normally
R201A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells
R83A
-
mutant with reduced activity, the mutant cannot suppress phytosphingosine accumulation, although the protein is expressed normally
W124A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells
W23A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells
Y142A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells
Y149A
-
inactive, the mutant cannot suppress phytosphingosine accumulation, although the protein is expressed normally
Y15A
-
phytosphingosine accumulates at low levels in the mutant compared with wild type cells