Information on EC 2.3.1.199 - very-long-chain 3-oxoacyl-CoA synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.3.1.199
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RECOMMENDED NAME
GeneOntology No.
very-long-chain 3-oxoacyl-CoA synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a very-long-chain acyl-CoA + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + coenzyme A
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
arachidonate biosynthesis IV (8-detaturase, lower eukaryotes)
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arachidonate biosynthesis V (8-detaturase, mammals)
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Biosynthesis of secondary metabolites
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Biosynthesis of unsaturated fatty acids
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Fatty acid elongation
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hydroxylated fatty acid biosynthesis (plants)
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icosapentaenoate biosynthesis III (8-desaturase, mammals)
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icosapentaenoate biosynthesis V (8-desaturase, lower eukaryotes)
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juniperonate biosynthesis
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sciadonate biosynthesis
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stearate biosynthesis I (animals and fungi)
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very long chain fatty acid biosynthesis I
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very long chain fatty acid biosynthesis II
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SYSTEMATIC NAME
IUBMB Comments
malonyl-CoA:very-long-chain acyl-CoA malonyltransferase (decarboxylating and thioester-hydrolysing)
This is the first 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. Multiple forms exist with differing preferences for the substrate, and thus the specific form expressed determines the local composition of very-long-chain fatty acids [6,7]. For example, the FAE1 form from the plant Arabidopsis thaliana accepts only 16 and 18 carbon substrates, with oleoyl-CoA (18:1) being the preferred substrate [5], while CER6 from the same plant prefers substrates with chain length of C22 to C32 [4,8]. cf. EC 1.1.1.330, very-long-chain 3-oxoacyl-CoA reductase, EC 4.2.1.134, very-long-chain (3R)-3-hydroxyacyl-[acyl-carrier protein] dehydratase, and EC 1.3.1.93, very-long-chain enoyl-CoA reductase
CAS REGISTRY NUMBER
COMMENTARY hide
88414-92-0
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
the enzyme is involved in the fatty acid elongation cycle consisting of the reaction steps of condensation, reduction, dehydration, and reduction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(11Z)-eicosenoyl-CoA + malonyl-CoA
?
show the reaction diagram
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?
a very-long-chain acyl-CoA + malonyl-CoA
a very-long-chain 3-oxoacyl-CoA + CO2 + coenzyme A
show the reaction diagram
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?
arachidoyl-CoA + malonyl-CoA
?
show the reaction diagram
behenoyl-CoA + malonyl-CoA
?
show the reaction diagram
cerotoyl-CoA + malonyl-CoA
?
show the reaction diagram
decanoyl-CoA + malonyl-CoA
?
show the reaction diagram
eicosenoyl-CoA + malonyl-CoA
?
show the reaction diagram
22:1DELTA13
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?
erucoyl-CoA + malonyl-CoA
?
show the reaction diagram
lauroyl-CoA + malonyl-CoA
?
show the reaction diagram
myristoyl-CoA + malonyl-CoA
?
show the reaction diagram
n-hexacosanoyl-CoA + malonyl-CoA
?
show the reaction diagram
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?
octanoyl-CoA + malonyl-CoA
?
show the reaction diagram
oleoyl-CoA + malonyl-CoA
?
show the reaction diagram
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in contrast to stearic acid-CoA, oleic acid-CoA serves as a less suitable substrate for elongation
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?
oleoyl-CoA + malonyl-CoA
CoA + 3-oxo-eicosenoyl-CoA + 3-oxo-erucoyl-CoA + CO2
show the reaction diagram
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preferred substrate
3-oxo-eicosenoyl-CoA is the major product
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?
palmitoleoyl-CoA + malonyl-CoA
?
show the reaction diagram
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?
palmitoyl-CoA + malonyl-CoA
3-oxostearoyl-CoA + CO2 + CoA
show the reaction diagram
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?
palmitoyl-CoA + malonyl-CoA
?
show the reaction diagram
stearoyl-CoA + malonyl-CoA
?
show the reaction diagram
stearoyl-CoA + malonyl-CoA
CoA + 3-oxo-eicosanoyl-CoA + CO2
show the reaction diagram
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major product
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?
very-long-chain acyl-CoA + malonyl-CoA
CoA + very-long-chain 3-oxoacyl-CoA + CO2
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
a very-long-chain acyl-CoA + malonyl-CoA
a very-long-chain 3-oxoacyl-CoA + CO2 + coenzyme A
show the reaction diagram
Q9H5J4
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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CoA, NADPH and ATP have no effect on the condensation activity of the recombinant enzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
mefluidide
metazachlor
perfluidone
additional information
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not inhibited by aristolochic acid
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
ELOVL6 activity in membrane fractions is enhanced in the presence of NADPH
additional information
the 3-ketoacyl-CoA reductase, KAR, the enzyme catalyzing the next step in metabolism after fatty acid elongase ELOVL6, largely stimulates ELOVL6 activity. Activity of purified enzyme ELOVL6 is enhanced by about 3fold in the presence of 3-ketoacyl-CoA reductase, KAR. This effect is KAR enzyme activity-independent, since it is observed in the absence of NADPH and in the poorly active or inactive KAR mutants, overview. ELOVL6 enzyme activity is also enhanced in a KAR enzyme activity-dependent manner
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.83
decanoyl-CoA
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in 10 mM Tris/maleic acid pH 6.7, 0.65 M mannitol and 0.36 mM EGTA, at 30°C
0.05
lauroyl-CoA
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in 10 mM Tris/maleic acid pH 6.7, 0.65 M mannitol and 0.36 mM EGTA, at 30°C
0.4
myristoyl-CoA
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in 10 mM Tris/maleic acid pH 6.7, 0.65 M mannitol and 0.36 mM EGTA, at 30°C
0.33
Octanoyl-CoA
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in 10 mM Tris/maleic acid pH 6.7, 0.65 M mannitol and 0.36 mM EGTA, at 30°C
0.00122 - 0.13
palmitoyl-CoA
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000032 - 0.00199
mefluidide
0.0076 - 0.114
metazachlor
0.00021 - 0.5
perfluidone
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.3
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
detected only in the elongating wild type cotton fibre cells
Manually annotated by BRENDA team
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highest expression of isoform KCS20
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
x * 29000, recombinant deglycosylated 3xFLAG-tagged enzyme, SDS-PAGE, x * 32000, recombinant glycosylated 3xFLAG-tagged enzyme, SDS-PAGE
43000
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x * 43000, SDS-PAGE
55000
x * 55000, calculated from amino acid sequence
56400
calculated from amino acid sequence
58300
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x * 58300, calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
deglycosylation is possibel with Endo H
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+-PDC column chromatography
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recombinant N-terminally 3xFLAG-tagged enzyme ELOVL6 from HEK-293 T cells by solubilization with Triton X-100 and affinity chromatography
the His6-tagged enzyme is purified by Ni2+-pentadentate chelator affinity matrix column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Arabidopsis thaliana and Brassica carinata
expressed in Nicotiana tabacum
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expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae and Nicotiana tabacum
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expressed in Saccharomyces cerevisiae elo3 deletion mutation strain W1536-5B and elo2 and elo3 double-deletion strain W1536
expressed in Saccharomyces cerevisiae strain InvSc1
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mutant enzymes are expressed in Saccharomyces cerevisiae
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recombinant expression of N-terminally 3xFLAG-tagged enzyme ELOVL6 in HEK-293 T cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CER6 mRNA increases to more than 7fold in 10 days post anthesis
isoform KCS20 mRNA expression is stimulated about 2fold by drought stress (air-drying for 6 h). Isoform KCS2/DAISY mRNA expression is stimulated about 4 fold at 200 mM mannitol, about 60fold at drought stress, about 3fold at 100 mM NaCl, and about 20fold at 0.1 mM abscisic acid
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light is required for expression and expression is increased by salt and drought treatments
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the ELO1 gene is rapidly induced in wild type cells that are supplemented with myristic acid
the ELO1 gene is repressed in wild type cells that are supplemented with palmitic acid and stearic acid
the expression of 1-aminocyclopropane-1-carboxylic acid synthase ACS1, CUT1L, and ATP-binding cassette transporter RCN1/OsABCG5 is induced predominantly in the outer part of roots under stagnant conditions
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C223A
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the mutant enzyme lacking the acylation site is unable to carry out decarboxylation of malonyl-CoA even when oleic acid-CoA is present
H391A
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the mutant enzyme lacking the acylation site is unable to carry out decarboxylation of malonyl-CoA even when oleic acid-CoA is present
H391K
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the mutant shows very low condensation activity
H391Q
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the mutant shows low condensation activity (25% activity compared to the wild type enzyme)
N424D
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the mutant shows low condensation activity
N424H
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the mutant enzyme lacking the acylation site is unable to carry out decarboxylation of malonyl-CoA even when oleic acid-CoA is present
S282A
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the mutant shows reduced activity with 20:1DELTA11 and erucic acid-CoA as substrates compared to the wild type enzyme
S282C
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the mutant shows increased activity with 20:1DELTA11 and erucic acid-CoA as substrates compared to the wild type enzyme
S282G
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the mutant shows wild type activity with 20:1DELTA11 and erucic acid-CoA as substrates
S282I
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the mutant is inactive
S282N
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the mutant is inactive
S282Q
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the mutant is inactive
S282T
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the mutant shows reduced activity with 20:1DELTA11 and erucic acid-CoA as substrates compared to the wild type enzyme
S282V
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the mutant is inactive
S282Y
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the mutant is inactive
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme ELOVL6 has no enzyme activity under solubilized conditions, reconstitution of ELOVL6 into proteoliposomes enables it to exhibit enzyme activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
human cytomegalovirus HMCV induces isoform ELOVL7 by more than 150fold. The induction is dependent on mTOR and SREBP-1. ELOVL7 knockdown or mTOR inhibition impairs HCMV-induced fatty acid elongation, HCMV particle release, and infectivity per particle. ELOVL7 overexpression enhances HCMV replication. During HCMV infection, mTOR activity is maintained by the viral protein pUL38. Expression of pUL38 is sufficient to induce ELOVL7, and pUL38-deficient virus is partially defective in ELOVL7 induction and fatty acid elongation
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