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Information on EC 2.3.1.199 - very-long-chain 3-oxoacyl-CoA synthase
for references in articles please use BRENDA:EC2.3.1.199
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.1 Transferring groups other than aminoacyl groups
2.3.1.199 very-long-chain 3-oxoacyl-CoA synthase
IUBMB Comments
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 , 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
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
- 2.3.1.199
-
vlcfas
-
polyunsaturated
- acyl-coas
-
desaturase
-
elovls
-
monounsaturated
- cuticular
- ceramide
-
erucic
-
pufas
- sphingolipids
- stearoyl-coa
-
oilseed
-
epicuticular
- adrenoleukodystrophy
-
eicosenoic
-
delta6
-
docosapentaenoic
-
napins
-
vlc-pufas
- leek
- suberins
- medicine
Reaction Schemes
showSynonyms
fatty acid elongase, elovl1, elovl7, 3-ketoacyl-coa synthase, fatty acid elongase 1, acyl-coa elongase, beta-ketoacyl-coa synthase, fa elongase, fae1 kcs, fatty acid elongation1, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-ketoacyl-CoA synthase
acyl-CoA elongase
At2g26640
beta-ketoacyl-CoA synthase
CER6
CER60
Cut1
EC 2.3.1.119
-
-
formerly, part transferred
-
ELO
ELo1
Elo1p
FAE1
Fatty acid elongase
fatty acid elongase 1
KCS
Kcs1
KCS11
KCS12
KCS19
KCS2
KCS20
KCS3
MALCE1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a very-long-chain acyl-CoA + malonyl-CoA = a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
(9Z)-tricosene biosynthesis, arachidonate biosynthesis IV (8-detaturase, lower eukaryotes), arachidonate biosynthesis V (8-detaturase, mammals), hydroxylated fatty acid biosynthesis (plants), icosapentaenoate biosynthesis III (8-desaturase, mammals), icosapentaenoate biosynthesis V (8-desaturase, lower eukaryotes), juniperonate biosynthesis, sciadonate biosynthesis, stearate biosynthesis I (animals), ultra-long-chain fatty acid biosynthesis, very long chain fatty acid biosynthesis I, 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
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CAS REGISTRY NUMBER
COMMENTARY
88414-92-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(11Z)-eicosenoyl-CoA + malonyl-CoA
CoA + 3-oxo-erucoyl-CoA + CO2
-
Substrates: -
Products: -
Products: -
?
(9Z,12Z)-octadec-9,12-dienoyl-CoA + malonyl-CoA
(11Z,14Z)-3-oxoeicosa-11,14-dienoyl-CoA + CO2 + coenzyme A
(9Z,12Z,15Z)-octadeca-9,12,15-trienoyl-CoA + malonyl-CoA
(11Z,14Z,17Z)-3-oxoeicosa-11,14,17-trienoyl-CoA + CO2 + coenzyme A
3-erucicoyl-CoA + malonyl-CoA
3-oxo-nervonoyl-CoA + CO2 + coenzyme A
-
Substrates: -
Products: -
Products: -
?
a very-long-chain acyl-CoA + malonyl-CoA
a very-long-chain 3-oxoacyl-CoA + CO2 + coenzyme A
Substrates: -
Products: -
Products: -
?
a very-long-chain acyl-CoA + malonyl-CoA + H+
a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
Substrates: -
Products: -
Products: -
?
eicosenoyl-CoA + malonyl-CoA
3-oxo-erucicoyl-CoA + CO2 + coenzyme A
-
Substrates: -
Products: -
Products: -
?
eicosenoyl-CoA + malonyl-CoA
?
Substrates: 22:1DELTA13
Products: -
Products: -
?
erucoyl-CoA + malonyl-CoA
CoA + 3-oxo-nervonoyl-CoA + CO2
-
Substrates: -
Products: -
Products: -
?
oleoyl-CoA + malonyl-CoA
?
-
Substrates: in contrast to stearic acid-CoA, oleic acid-CoA serves as a less suitable substrate for elongation
Products: -
Products: -
?
oleoyl-CoA + malonyl-CoA
CoA + 3-oxo-eicosenoyl-CoA + 3-oxo-erucoyl-CoA + CO2
-
Substrates: preferred substrate
Products: 3-oxo-eicosenoyl-CoA is the major product
Products: 3-oxo-eicosenoyl-CoA is the major product
?
palmitoyl-CoA + malonyl-CoA
3-oxostearoyl-CoA + CO2 + CoA
Substrates: -
Products: -
Products: -
?
stearoyl-CoA + malonyl-CoA
CoA + 3-oxo-eicosanoyl-CoA + CO2
-
Substrates: -
Products: major product
Products: major product
?
(9Z)-hexadec-9-enoyl-CoA + malonyl-CoA
(11Z)-3-oxooctadec-11-enoyl-CoA + CO2 + coenzyme A
Substrates: -
Products: -
Products: -
ir
(9Z)-hexadec-9-enoyl-CoA + malonyl-CoA
(11Z)-3-oxooctadec-11-enoyl-CoA + CO2 + coenzyme A
Substrates: -
Products: -
Products: -
ir
(9Z,12Z)-octadec-9,12-dienoyl-CoA + malonyl-CoA
(11Z,14Z)-3-oxoeicosa-11,14-dienoyl-CoA + CO2 + coenzyme A
Substrates: -
Products: -
Products: -
ir
(9Z,12Z)-octadec-9,12-dienoyl-CoA + malonyl-CoA
(11Z,14Z)-3-oxoeicosa-11,14-dienoyl-CoA + CO2 + coenzyme A
Substrates: -
Products: -
Products: -
ir
(9Z,12Z,15Z)-octadeca-9,12,15-trienoyl-CoA + malonyl-CoA
(11Z,14Z,17Z)-3-oxoeicosa-11,14,17-trienoyl-CoA + CO2 + coenzyme A
Substrates: -
Products: -
Products: -
?
(9Z,12Z,15Z)-octadeca-9,12,15-trienoyl-CoA + malonyl-CoA
(11Z,14Z,17Z)-3-oxoeicosa-11,14,17-trienoyl-CoA + CO2 + coenzyme A
Substrates: -
Products: -
Products: -
?
a very-long-chain acyl-CoA + malonyl-CoA
a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
-
Substrates: -
Products: -
Products: -
?
a very-long-chain acyl-CoA + malonyl-CoA
a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
Substrates: -
Products: -
Products: -
?
arachidoyl-CoA + malonyl-CoA
?
-
Substrates: best substrate for At4g34510
Products: -
Products: -
?
arachidoyl-CoA + malonyl-CoA
?
-
Substrates: 25% activity compared to oleoyl-CoA
Products: -
Products: -
?
erucoyl-CoA + malonyl-CoA
?
Substrates: 20:1DELTA11
Products: -
Products: -
?
myristoyl-CoA + malonyl-CoA
?
-
Substrates: best substrate
Products: -
Products: -
?
myristoyl-CoA + malonyl-CoA
?
-
Substrates: best substrate
Products: -
Products: -
?
palmitoyl-CoA + malonyl-CoA
?
-
Substrates: best substrate for KCS1
Products: -
Products: -
?
stearoyl-CoA + malonyl-CoA
?
-
Substrates: best substrate for At2g26640 and FAE1
Products: -
Products: -
?
very-long-chain acyl-CoA + malonyl-CoA
CoA + very-long-chain 3-oxoacyl-CoA + CO2
-
Substrates: -
Products: -
Products: -
?
very-long-chain acyl-CoA + malonyl-CoA
CoA + very-long-chain 3-oxoacyl-CoA + CO2
-
Substrates: -
Products: -
Products: -
?
very-long-chain acyl-CoA + malonyl-CoA
CoA + very-long-chain 3-oxoacyl-CoA + CO2
-
Substrates: -
Products: -
Products: -
?
very-long-chain acyl-CoA + malonyl-CoA
CoA + very-long-chain 3-oxoacyl-CoA + CO2
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: At1g01120 (KCS1) and At2g26640 have broad substrate specificities when assayed with saturated and monounsaturated C16 to C24 acyl-CoAs while At4g34510 is specific for saturated fatty acyl-CoA substrates. KCS1 is most active with palmitic acid, palmitoleic acid, stearic acid, and arachidic acid but has very little activity with oleic acid and acyl chains longer than C20. At4g34510 is specific for saturated acyl-CoAs up to C22. FAE1 uses palmitic acid, palmitoleic acid, stearic acid, oleic acid, arachidic acid, 20:1, behenic acid, erucic acid, and lignoceric acid as substratesis and is specific for acyl-CoAs of 16 and 18 carbons in length
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows highest activity towards saturated and monounsaturated C16 and C18. In the absence of an acyl-CoA substrate, the enzyme is unable to carry out decarboxylation of malonyl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows no activity with polyunsaturated linoleic acid and alpha-linolenic acid and little or no activity with acyl-CoAs having 22 carbons or longer in chain length
Products: -
Products: -
?
additional information
?
-
Substrates: the effect of CER2-LIKE1 and CER2-LIKE2 proteins on fatty acid elongation is limited to specific condensing enzyme partners, and CER2-LIKE proteins either have their own unique substrate specificity, or a unique effect on the substrate specificity of the condensing enzyme with which they function
Products: -
Products: -
?
additional information
?
-
Substrates: the effect of CER2-LIKE1 and CER2-LIKE2 proteins on fatty acid elongation is limited to specific condensing enzyme partners, and CER2-LIKE proteins either have their own unique substrate specificity, or a unique effect on the substrate specificity of the condensing enzyme with which they function
Products: -
Products: -
?
additional information
?
-
Substrates: almost no activity with palmitic acid and 17:1DELTA9
Products: -
Products: -
?
additional information
?
-
-
Substrates: almost no activity with palmitic acid and 17:1DELTA9
Products: -
Products: -
?
additional information
?
-
Substrates: almost no activity with palmitic acid and 17:1DELTA9
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme is able to elongate the C16-acyl-CoA up to C26-acyl-CoA
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is able to elongate the C16-acyl-CoA up to C26-acyl-CoA
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with saturated and unsaturated fatty acids longer than C16
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is specific for acyl chain lengths between 16 and 20 carbons
Products: -
Products: -
?
additional information
?
-
-
Substrates: subclade A members KCS1 and KCS9 generally show higher accumulation of shorter products relative to KCS2 and KCS8 from subclade B. KCS2 and PCS8 show preference toward the production of saturated VLCFAs and cis-omega7-monounsaturated substrates. KCS1 and KCS9 show higher production of cis-omega9-monounsaturated fatty acids. CS4 accumulates both shorter and cis-omega9-monounsaturated VLCFAs, but also high levels of saturated products
Products: -
Products: -
-
additional information
?
-
-
Substrates: isoform KCS7 is responsible for the production of C20:1 to C24:1 VLCFA
Products: -
Products: -
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a very-long-chain acyl-CoA + malonyl-CoA
a very-long-chain 3-oxoacyl-CoA + CO2 + coenzyme A
Substrates: -
Products: -
Products: -
?
a very-long-chain acyl-CoA + malonyl-CoA + H+
a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
Substrates: -
Products: -
Products: -
?
a very-long-chain acyl-CoA + malonyl-CoA
a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
-
Substrates: -
Products: -
Products: -
?
a very-long-chain acyl-CoA + malonyl-CoA
a very-long-chain 3-oxoacyl-CoA + CO2 + CoA
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
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
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alachlor
-
reduces VLCFA elongation in isoforms KCS1, KSC2, KSC4 by 15%-60%
anilofos
-
reduces VLCFA elongation in isoforms KCS1, KSC2, KSC4 by 20-60%
-
fentrazamide
-
reduces VLCFA elongation in isoforms KCS1, KSC2, KSC4 by more than 70%
-
flufenacet
-
reduces VLCFA elongation in isoforms KCS1, KSC2, KSC4 by more than 60%
mefluidide
-
selective inhibitor of KCS1, CER6, and CER60 enzyme activities in vivo. FAE1 and KCS2 are inhibited by mefluidide only slightly. At 0.1 mM mefluidide, isozymes FAE1, KCS1, KCS2, KCS20, CER60, and CER6 are inhibited by 5.1%, 91%, 0.3%, 26.9%, 71.8%, 51.2% respectively
metazachlor
-
selective inhibitor of KCS1, CER6, and CER60 enzyme activities in vivo. Strong micromolar inhibitor of FAE1 and KCS2. At 0.1 mM metazachlor, isozymes FAE1, KCS1, KCS2, KCS20, CER60, CER6, and KCS17 are inhibited by 95.7%, 93%, 82.4%, 97.5%, 100%, 100%, and 100%, respectively
perfluidone
-
selective inhibitor of KCS1, CER6, and CER60 enzyme activities in vivo. Strong micromolar inhibitor of FAE1 and KCS2
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acanthosis Nigricans
De novo mutation in ELOVL1 causes ichthyosis, acanthosis nigricans, hypomyelination, spastic paraplegia, high frequency deafness and optic atrophy.
Adrenoleukodystrophy
Enzymatic characterization of ELOVL1, a key enzyme in very long-chain fatty acid synthesis.
Adrenoleukodystrophy
The role of ELOVL1 in very long-chain fatty acid homeostasis and X-linked adrenoleukodystrophy.
Breast Neoplasms
Estrogen Enhances the Expression of the Polyunsaturated Fatty Acid Elongase Elovl2 via ER? in Breast Cancer Cells.
Breast Neoplasms
Novel theranostic opportunities offered by characterization of altered membrane lipid metabolism in breast cancer progression.
Corneal Opacity
Very long-chain tear film lipids produced by fatty acid elongase ELOVL1 prevent dry eye disease in mice.
Deafness
De novo mutation in ELOVL1 causes ichthyosis, acanthosis nigricans, hypomyelination, spastic paraplegia, high frequency deafness and optic atrophy.
Deafness
Reduced chain length in myelin sphingolipids and poorer motor coordination in mice deficient in the fatty acid elongase Elovl1.
Demyelinating Diseases
Dicer ablation in oligodendrocytes provokes neuronal impairment in mice.
Dermatitis
IFN-? Reduces Epidermal Barrier Function by Affecting Fatty Acid Composition of Ceramide in a Mouse Atopic Dermatitis Model.
Dry Eye Syndromes
Improvement of Evaporative Dry Eye With Meibomian Gland Dysfunction in Model Mice by Treatment With Ophthalmic Solution Containing Mineral Oil.
Dry Eye Syndromes
Very long-chain tear film lipids produced by fatty acid elongase ELOVL1 prevent dry eye disease in mice.
Fatty Liver
Fatty acid elongase-5 (Elovl5) regulates hepatic triglyceride catabolism in obese C57BL/6J mice.
Hyperglycemia
Disrupted sphingolipid metabolism following acute clozapine and olanzapine administration.
Hyperkeratosis, Epidermolytic
Ichthyosis molecular fingerprinting shows profound TH17 skewing and a unique barrier genomic signature.
Ichthyosis
De novo mutation in ELOVL1 causes ichthyosis, acanthosis nigricans, hypomyelination, spastic paraplegia, high frequency deafness and optic atrophy.
Ichthyosis
Ichthyosis molecular fingerprinting shows profound TH17 skewing and a unique barrier genomic signature.
Ichthyosis
Reduced chain length in myelin sphingolipids and poorer motor coordination in mice deficient in the fatty acid elongase Elovl1.
Infections
Fatty Acid elongase 7 catalyzes lipidome remodeling essential for human cytomegalovirus replication.
Infections
Weighted Gene Co-Expression Network Analysis Identifies Key Modules and Hub Genes Associated with Mycobacterial Infection of Human Macrophages.
Insulin Resistance
Crucial role of a long-chain fatty acid elongase, Elovl6, in obesity-induced insulin resistance.
Insulin Resistance
Dysregulation of microRNA-125a contributes to obesity-associated insulin resistance and dysregulates lipid metabolism in mice.
Insulin Resistance
Macrophage elovl6 deficiency ameliorates foam cell formation and reduces atherosclerosis in low-density lipoprotein receptor-deficient mice.
Insulin Resistance
Role of fatty acid elongase Elovl6 in the regulation of energy metabolism and pathophysiological significance in diabetes.
Macular Degeneration
Loss of ER retention and sequestration of the wild-type ELOVL4 by Stargardt disease dominant negative mutants.
Multiple Myeloma
The fatty acid elongase ELOVL6 regulates bortezomib resistance in multiple myeloma.
Neoplasms
Differences in elongation of very long chain fatty acids and fatty acid metabolism between triple-negative and hormone receptor-positive breast cancer.
Neoplasms
Identification of hub genes and key pathways associated with the progression of gynecological cancer.
Neoplasms
Novel Lipogenic Enzyme ELOVL7 Is Involved in Prostate Cancer Growth through Saturated Long-Chain Fatty Acid Metabolism.
Neoplasms
Reactivation of androgen receptor-regulated lipid biosynthesis drives the progression of castration-resistant prostate cancer.
Neoplasms
Signatures of Adverse Pathological Features, Androgen Insensitivity and Metastatic Potential in Prostate Cancer.
Neoplasms
Systematic integration of molecular profiles identifies miR-22 as a regulator of lipid and folate metabolism in breast cancer cells.
Neurocutaneous Syndromes
Reduced chain length in myelin sphingolipids and poorer motor coordination in mice deficient in the fatty acid elongase Elovl1.
Non-alcoholic Fatty Liver Disease
The IGF2 mRNA binding protein p62/IGF2BP2-2 induces fatty acid elongation as a critical feature of steatosis.
Obesity
Ablation of the very-long-chain fatty acid elongase ELOVL3 in mice leads to constrained lipid storage and resistance to diet-induced obesity.
Obesity
Fatty acid elongase-5 (Elovl5) regulates hepatic triglyceride catabolism in obese C57BL/6J mice.
Obesity
Regulation of hepatic fatty acid elongase and desaturase expression in diabetes and obesity.
Optic Atrophy
De novo mutation in ELOVL1 causes ichthyosis, acanthosis nigricans, hypomyelination, spastic paraplegia, high frequency deafness and optic atrophy.
Paraplegia
De novo mutation in ELOVL1 causes ichthyosis, acanthosis nigricans, hypomyelination, spastic paraplegia, high frequency deafness and optic atrophy.
Paraplegia
Reduced chain length in myelin sphingolipids and poorer motor coordination in mice deficient in the fatty acid elongase Elovl1.
Parkinson Disease
Association of GALC, ZNF184, IL1R2 and ELOVL7 With Parkinson's Disease in Southern Chinese.
Parkinson Disease
Transcriptomic signatures of brain regional vulnerability to Parkinson's disease.
Prostatic Neoplasms
ELOVL5 is a critical and targetable fatty acid elongase in prostate cancer.
Prostatic Neoplasms
Novel Lipogenic Enzyme ELOVL7 Is Involved in Prostate Cancer Growth through Saturated Long-Chain Fatty Acid Metabolism.
Prostatic Neoplasms
The chromatin remodeling protein BRG1 links ELOVL3 trans-activation to prostate cancer metastasis.
Protein Deficiency
Enzymatic characterization of ELOVL1, a key enzyme in very long-chain fatty acid synthesis.
Rubella
Regulation of FATTY ACID ELONGATION1 expression and production in Brassica oleracea and Capsella rubella.
Starvation
Identification of a ?6 fatty acid elongase gene for arachidonic acid biosynthesis localized to the endoplasmic reticulum in the green microalga Myrmecia incisa Reisigl.
very-long-chain 3-oxoacyl-coa synthase deficiency
Reduced chain length in myelin sphingolipids and poorer motor coordination in mice deficient in the fatty acid elongase Elovl1.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.83
decanoyl-CoA
-
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
-
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
-
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
-
in 10 mM Tris/maleic acid pH 6.7, 0.65 M mannitol and 0.36 mM EGTA, at 30°C
0.13
palmitoyl-CoA
-
in 10 mM Tris/maleic acid pH 6.7, 0.65 M mannitol and 0.36 mM EGTA, at 30°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000032
mefluidide
Arabidopsis thaliana
-
isozyme CER6, pH and temperature not specified in the publication
0.00199
mefluidide
Arabidopsis thaliana
-
isozyme FAE1, pH and temperature not specified in the publication
0.0076
metazachlor
Arabidopsis thaliana
-
isozyme FAE1, pH and temperature not specified in the publication
0.114
metazachlor
Arabidopsis thaliana
-
isozyme CER6, pH and temperature not specified in the publication
0.00021
perfluidone
Arabidopsis thaliana
-
isozyme CER6, pH and temperature not specified in the publication
0.5
perfluidone
Arabidopsis thaliana
-
IC50 above 0.5 mM, isozyme FAE1, pH and temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
detected only in the elongating wild type cotton fibre cells
brenda
isoform KCS3 is specifically expressed in guard cells of young tissues
brenda
additional information
-
isoform KCS20 and KCS2/DAISY transcripts are approximately 4 and 2fold higher in epidermal peels than in stem
brenda
highest expression in aerial part of 2-week-old seedlings
brenda
additional information
no expression fopund in root
brenda
additional information
not detected in root, leaf, stem, and ovule
brenda
additional information
-
not detected in root, leaf, stem, and ovule
brenda
additional information
-
enzyme is specifically expressed in the outermost cell layer of young lateral organs
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
suppression of CUT1 in transgenic Arabidopsis plants results in waxless (eceriferum) stems and siliques as well as conditional male sterility. In CUT1-suppressed plants, the C24 chain-length wax components predominate. Both decarbonylation and acyl reduction pathways are down-regulated in cut1-suppressed plants
malfunction
-
complete loss of KCS1 expression results in decreases of up to 80% in the levels of C26 to C30 wax alcohols and aldehydes, while smaller effects are observed on the major wax components, i.e. the C29 alkanes and C29 ketones on leaves, stems and siliques. The loss of KCS1 expression does not result in complete loss of any individual wax component or significantly decrease the total wax load
malfunction
-
FAE1 misexpression plants are similar to the wild type but display an essentially glabrous phenotype, owing to the selective death of trichome cells. Nuclei of arrested trichome cells in FAE1 misexpression plants cell-autonomously accumulate high levels of DNA damage, including double-strand breaks characteristic of lipoapoptosis
malfunction
-
complete loss of isoform KCS20 and KCS2 genes decreases the total wax content in stems and leaves by 20% and 15%, respectively. Kcs20 kcs2/daisy-1 double mutants exhibit significant reduction of C22 and C24 very-long-chain fatty acid derivatives but accumulation of C20 very-long-chain fatty acid derivatives in aliphatic suberin
malfunction
-
null mutations in ELO3 result in accumulation of labeled precursors into inositol phosphoceramide, with little labeling in the more complex mannosylated sphingolipids, whereas disruption of ELO2 results in reduced levels of all sphingolipids. Mutations in ELO3 lead to elevated levels of C20 and C22 fatty acids (most abundant species is behenic acid which averages 3.1% of the total fatty acyl mass, a 10fold increase over wild type levels). ELO3 disruption results in an approximate 20% increase in the total levels of very long chain species. Sharply reduced levels of cerotic acid (approximately 20% wild type levels) and hydroxy-cerotic acid (approximately 40% of wild type levels) are found in an elo2 mutant strain
malfunction
-
enzyme mutations reduce the amount of wax, but not the total load of cutin in leaf blades, and result in an increased rate of water loss. Enzyme defects affect cuticle structure, water barrier properties of the cuticle and infection by the powdery mildew fungus
malfunction
enzyme isoform KCS19 mutants show seed fusion phenotypes and altered chain length distributions in seed suberin
malfunction
enzyme isoform KCS3 mutants have redundant effects on sepal fusion and bud wax composition
malfunction
enzyme isoform KCS12 mutants have redundant effects on sepal fusion and bud wax composition
metabolism
the enzyme is involved in the fatty acid elongation cycle consisting of the reaction steps of condensation, reduction, dehydration, and reduction
metabolism
the enzyme is involved in docosahexaenoic acid synthesis pathway in the teleost Solea senegalensis
metabolism
the enzyme is involved in very-long-chain fatty acid elongation beyond C22. Elongation beyond C24 requires the participation of CER2
physiological function
a MALCE1 gene-silenced strain exhibits a low content of octadecanoic acid and a high content of hexadecanoic acid
physiological function
the enzyme has strong capability for improving the erucic acid content
physiological function
the enzyme plays a role in the production of epicuticular and pollen coat lipids more than 28 carbons long
physiological function
-
the CUT1 enzyme is required for cuticular wax biosynthesis and pollen fertility
physiological function
-
the enzyme plays a role in wax biosynthesis and is involved in both, the decarbonylation and acyl-reduction wax synthesis pathways
physiological function
-
enzymic activity of FAE1 is required to suppress trichome development. The enzyme plays a role in the biosynthesis of cutin
physiological function
-
FAE1 is the rate-limiting enzyme for very-long-chain fatty acid biosynthesis in Arabidopsis seed
physiological function
-
isoforms KCS20 and KCS2/DAISY are functionally redundant in the two-carbon elongation to C22 very-long-chain fatty acid that is required for cuticular wax and root suberin biosynthesis
physiological function
-
the enzyme is required for epicuticular wax in bolting stems
physiological function
-
Elo2p is involved in the elongation of fatty acids up to 24 carbons and has the highest affinity for substrates with chain lengths less than 22 carbons. Elo3p has a broader substrate specificity and is essential for the conversion of 24-carbon acids to 26-carbon species
physiological function
3-ketoacyl-CoA reductase, KAR, regulates enzyme ELOVL6 via two modes: in the first mode, KAR may induce conformational changes in ELOVL6 to become a structure that can undergo catalysis. In the second mode, conversion of 3-oxoacyl-CoA to 3-hydroxyacyl-CoA by KAR may facilitate release of the product from the presumed ELOVL6-KAR complex
physiological function
-
Elovl1 knockout mice die shortly after birth due to epidermal barrier defects. The lipid lamellae in the stratum corneum are largely diminished in these mice. In the epidermis of the Elovl1-null mice, the levels of Cers with more than C26 fatty acids are decreased, while those of Cers with less than C24 fatty acids are increased. The levels of C24 sphingomyelin are reduced, accompanied by an increase in C20 sphingomyelin levels. Ceramide synthases, CerS2 and CerS3, expressed in an epidermal layer-specific manner, regulate Elovl1 to produce acyl coenzyme As with different chain lengths
physiological function
rosette leafs of CER2-LIKE1 mutant plants show increased levels of C30-derived waxes and less C32-derived C31 alkane. Transferase CER2 and CER2-LIKE1-1 have redundant functions in elongation past C28 in leaves. CER2-LIKE1 partially rescues the stem wax-deficient phenotype of cer2-5. Yeast cells coexpressing condensing enzyme CER6 and CER2-LIKE1 synthesize C28, C30, C32, and C34 very-long-chain fatty acids
physiological function
transferase CER2 and CER2-LIKE2 have semiredundant functions required for male fertility
physiological function
in rice lines in which the gene encoding a fatty acid elongase, CUT1L, is silenced, both 1-aminocyclopropane-1-carboxylic acid synthase ACS1 expression and aerenchyma formation are reduced. The expression of ACS1, CUT1L, and ATP-binding cassette transporter RCN1/OsABCG5 is induced predominantly in the outer part of roots under stagnant conditions. In rice under oxygen-deficient conditions, very-long-chain fatty acids increase ethylene production by promoting 1-aminocyclopropane-1-carboxylic acid biosynthesis in the outer part of roots, which, in turn, induces aerenchyma formation in the root cortex
physiological function
-
elongase Onion2 mutants produce very small shoots in which leaves are fused to each other, and cease growing after germination. The midrib of Onion2 mutant leaf blades is not developed correctly. The amount of saturated very-long-chain fatty acids of C = 20, 24, 26, 28 and 30 is reduced in the mutant shoots
physiological function
enzyme overexpression increases the cuticular wax load and the quantity of C30-C34 fatty acids in rice leaves. The enzyme is involved in reproductive and vegetative organ development processes as well as epicuticular wax formation in rice
physiological function
KCS10 affects leaf permeability by mediating epicuticular wax accumulation. KCS10 overexpression mainly increases the amount of C29 and C31 n-alkanes, increases compact platelet-like crystal deposition and promotes primary alcohol biosynthesis. Overexpression in tobacco and tomato fruits induces the formation of coiled-rodlet-like crystals and increased n-alkane content through decarbonylation pathways. In transgenic tobacco, overexpression of KCS10 enhances drought tolerance by limiting nonstomatal water loss, improving photosynthesis, and maintaining osmotic potential under drought stress
physiological function
-
upon overexpression in Saccharomyces cerevisiae and Arabidopsis thaliana, only isoform KCS7 possesses the ability to facilitate the biosynthesis of C24:1
physiological function
isoform KCS knockout mutants display reduced total wax and wax crystals, particularly alkanes. KCS19 overexpression increases these components and wax crystals. The cuticle permeability is higher for the KCs19 mutants compared to the wild-type. KCS19 overexpression enhances drought and salt tolerance. Disrupting KCS19 increases C18 species and decreases C20 and longer species in seed fatty acids
physiological function
transgenic plants overexpressing KCS13 show increased sensitivity to cold stress. Expression of KCS13 increases the sensitivity of yeast cells to cold stress. Overexpression of KCS13 may cause remodeling of lipids in the endoplasmic reticulum and biosynthesis of lipid-derived jasmonic acid in chloroplasts
physiological function
-
seed-specific expression of KCS11 in Arabidopsis thaliana and in camelina leads to the accumulation of erucic acid (22:1) and nervonic acid (24:1), up to 5% nervonic acid are found
physiological function
-
in a Tnt1 insertion line in gene Medtr3g105550, leaves show sparser epicuticular wax crystals on the surface and increased water permeability compared with wild-typeIn mutant leaves, the percentage of C20:0, C22:0, and C24:0 fatty acids is significantly increased, the amount of cuticular wax is markedly reduced, and wax constituents are altered
physiological function
-
overexpression of Vitis vinifera KCS11 increases the tolerance to salt stress in Arabidopsis thaliana during the germination and seedling stages
physiological function
KCS11 insertion mutant shows increased sensitivity to salt stress at the germination stage
physiological function
in a spontaneous wax-deficient mutant, all wax monomers longer than 26 carbons are significantly decreased. All aerial organs of the the mutant plants are glossy green
physiological function
changes in isoform KCS3 expression mainly affect wax production. Mutants of KCS3 are hypersensitive to drought stress. The double-mutant lacking KCS3/KCS12 has significantly increased wax and cutin contents compared to either single-mutant, exhibits a fiddlehead phenotype and has decreased fertility. Cuticle permeability is greater for the double-mutant than for the single mutants
physiological function
the enzyme isoform KCS 19 is involved in seed coat formation. The enzyme is involved in the elongation of C18 or longer hydrocarbon chains in young, actively expanding tissues
physiological function
the enzyme isoform KCS3 has redundant function in flower development and is involved in the elongation of C18 or longer hydrocarbon chains in young, actively expanding tissues
physiological function
the enzyme isoform 12 has redundant function in flower development and is involved in the elongation of C18 or longer hydrocarbon chains in young, actively expanding tissues
physiological function
isoforms KCS12 overexpressing lines have fused floral organs because of abnormal cuticle biosynthesis. KCS12 expression is negatively related to wax and cutin accumulation in rosette leaves. Mutants of KCS12 are hypersensitive to drought stress. The double-mutant lacking KCS3/KCS12 has significantly increased wax and cutin contents compared to either single-mutant, exhibits a fiddlehead phenotype and has decreased fertility. Cuticle permeability is greater for the double-mutant than for the single mutants
physiological function
-
a MALCE1 gene-silenced strain exhibits a low content of octadecanoic acid and a high content of hexadecanoic acid
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29000
x * 29000, recombinant deglycosylated 3xFLAG-tagged enzyme, SDS-PAGE, x * 32000, recombinant glycosylated 3xFLAG-tagged enzyme, SDS-PAGE
32000
32000
x * 29000, recombinant deglycosylated 3xFLAG-tagged enzyme, SDS-PAGE, x * 32000, recombinant glycosylated 3xFLAG-tagged enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 29000, recombinant deglycosylated 3xFLAG-tagged enzyme, SDS-PAGE, x * 32000, recombinant glycosylated 3xFLAG-tagged enzyme, SDS-PAGE
?
-
x* 57800, isoform KCS4, x * 56800, isoform KCS7, x * 59100, isoform KCS8, calculated from sequence
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C223A
-
the mutant enzyme lacking the acylation site is unable to carry out decarboxylation of malonyl-CoA even when oleic acid-CoA is present
H391A
-
the mutant enzyme lacking the acylation site is unable to carry out decarboxylation of malonyl-CoA even when oleic acid-CoA is present
H391Q
-
the mutant shows low condensation activity (25% activity compared to the wild type enzyme)
N424H
-
the mutant enzyme lacking the acylation site is unable to carry out decarboxylation of malonyl-CoA even when oleic acid-CoA is present
S282A
-
the mutant shows reduced activity with 20:1DELTA11 and erucic acid-CoA as substrates compared to the wild type enzyme
S282C
-
the mutant shows increased activity with 20:1DELTA11 and erucic acid-CoA as substrates compared to the wild type enzyme
S282G
-
the mutant shows wild type activity with 20:1DELTA11 and erucic acid-CoA as substrates
S282T
-
the mutant shows reduced activity with 20:1DELTA11 and erucic acid-CoA as substrates compared to the wild type enzyme
L131K
-
mutation of KCS1 to the corresponding residue from KCS2, activity toward cis-monounsaturated fatty acids is reduced
L131K/W277C
-
mutation of KCS1 to the corresponding residue from KCS2, activity toward cis-monounsaturated fatty acids is reduced. the double mutation has synergistic effects
R275L
-
mutation of KCS1 to the corresponding residue from KCS2, results in a product profile identical to KCS1 wild-type
R283C
-
mutation of KCS4 to the corresponding residue from KCS2, reduces the production of monounsaturated VLCFAs
T137K
-
mutation of KCS4 to the corresponding residue from KCS2, reduces the production of monounsaturated VLCFAs and increases production of saturated C28 VLCFA
T137K/R283C
-
mutation of KCS4 to the corresponding residues from KCS2, converts the overall substrate preference of KCS4 almost completely to that of KCS2
W277C
-
mutation of KCS1 to the corresponding residue from KCS2, activity toward cis-monounsaturated fatty acids is reduced
additional information
additional information
-
construction of chimeras to swap smaller regions of KCS2 with the corresponding region from KCS1. The first 129 residues swapped between KCS1 and KCS2 are not sufficient to modify substrate specificity. The first 277 residues from KCS1 are sufficient for converting the substrate specificity of KCS2 to KCS1. The transmembrane domain does not affect substrate specificity. Helix-4 is important in conferring activity toward monounsaturated substrates
additional information
-
strains containing mutant forms of elo1 with deletion of fatty acid synthase 2 cannot elongate myristic acid but palmitic acid
additional information
-
strains containing mutant forms of elo1 with deletion of fatty acid synthase 2 cannot elongate myristic acid but palmitic acid
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae BY4741 elo3 mutant cells
expressed in Saccharomyces cerevisiae elo3 deletion mutation strain W1536-5B and elo2 and elo3 double-deletion strain W1536
recombinant expression of N-terminally 3xFLAG-tagged enzyme ELOVL6 in HEK-293 T cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
functional expression in yeast Saccharomyces cerevisiae results in the accumulation of 18-, 19-, and 20-carbon monounsaturated fatty acids and eicosanoic acid. The transformant efficiently elongates exogenous 9-hexadecenoic acid, 9,12-octadecadienoic acid, and 9,12,15-octadecatrienoic acid
in fasting conditions the effect of lipid level possibly prevails over or interacted with fatty acid composition in regulating the expression of elovl5, which is down-regulated in the liver of fish fed the high lipid diets
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
-
KCS13 expression levels in leaves are reduced by cold-stress treatment at 4°C
light is required for expression and expression is increased by salt and drought treatments
-
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
upon drought stress, the expression level in leaf increases 6fold and 4.5fold at 4 and 8 h, respectively
upon drought stress, the expression level in root decreases significantly
functional expression in yeast Saccharomyces cerevisiae results in the accumulation of 18-, 19-, and 20-carbon monounsaturated fatty acids and eicosanoic acid. The transformant efficiently elongates exogenous 9-hexadecenoic acid, 9,12-octadecadienoic acid, and 9,12,15-octadecatrienoic acid
functional expression in yeast Saccharomyces cerevisiae results in the accumulation of 18-, 19-, and 20-carbon monounsaturated fatty acids and eicosanoic acid. The transformant efficiently elongates exogenous 9-hexadecenoic acid, 9,12-octadecadienoic acid, and 9,12,15-octadecatrienoic acid
-
-
the ELO1 gene is rapidly induced in wild type cells that are supplemented with myristic acid
-
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 ELO1 gene is repressed in wild type cells that are supplemented with palmitic acid and stearic acid
-
-
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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
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dittrich, F.; Zajonc, D.; Huhne, K.; Hoja, U.; Ekici, A.; Greiner, E.; Klein, H.; Hofmann, J.; Bessoule, J.J.; Sperling, P.; Schweizer, E.
Fatty acid elongation in yeast. Biochemical characteristics of the enzyme system and isolation of elongation-defective mutants
Eur. J. Biochem.
252
477-485
1998
Saccharomyces cerevisiae, Saccharomyces cerevisiae X2180-1A
brenda
Blacklock, B.J.; Kelley, D.; Patel, S.
A fatty acid elongase ELO with novel activity from Dictyostelium discoideum
Biochem. Biophys. Res. Commun.
374
226-230
2008
Dictyostelium discoideum (Q54CJ4), Dictyostelium discoideum, Dictyostelium discoideum AX3 (Q54CJ4)
brenda
Sakuradani, E.; Nojiri, M.; Suzuki, H.; Shimizu, S.
Identification of a novel fatty acid elongase with a wide substrate specificity from arachidonic acid-producing fungus Mortierella alpina 1S-4
Appl. Microbiol. Biotechnol.
84
709-716
2009
Mortierella alpina (C8KHM6), Mortierella alpina, Mortierella alpina 1S-4 (C8KHM6), Mortierella alpina 1S-4
brenda
Fujisawa, M.; Watanabe, M.; Choi, S.K.; Teramoto, M.; Ohyama, K.; Misawa, N.
Enrichment of carotenoids in flaxseed (Linum usitatissimum) by metabolic engineering with introduction of bacterial phytoene synthase gene crtB
J. Biosci. Bioeng.
105
636-641
2008
Crambe hispanica subsp. abyssinica (Q32VC2)
brenda
Blacklock, B.; Jaworski, J.
Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases
Biochem. Biophys. Res. Commun.
346
583-590
2006
Arabidopsis thaliana
brenda
Kunst, L.; Clemens, S.; Hooker, T.
Expression of the wax-specific condensing enzyme CUT1 in Arabidopsis
Biochem. Soc. Trans.
28
651-654
2000
Arabidopsis thaliana
brenda
Ghanevati, M.; Jaworski, J.
Engineering and mechanistic studies of the Arabidopsis FAE1 beta-ketoacyl-CoA synthase, FAE1 KCS
Eur. J. Biochem.
269
3531-3539
2002
Arabidopsis thaliana
brenda
Katavic, V.; Barton, D.; Giblin, E.; Reed, D.; Kumar, A.; Taylor, D.
Gaining insight into the role of serine 282 in B. napus FAE1 condensing enzyme
FEBS Lett.
562
118-124
2004
Brassica napus
brenda
Toke, D.; Martin, C.
Isolation and characterization of a gene affecting fatty acid elongation in Saccharomyces cerevisiae
J. Biol. Chem.
271
18413-18422
1996
Saccharomyces cerevisiae, Saccharomyces cerevisiae W3031B
brenda
Oh, C.; Toke, D.; Mandala, S.; Martin, C.
ELO2 and ELO3, homologues of the Saccharomyces cerevisiae ELO1 gene, function in fatty acid elongation and are required for sphingolipid formation
J. Biol. Chem.
272
17376-17384
1997
Saccharomyces cerevisiae
brenda
Qin, Y.; Pujol, F.; Hu, C.; Feng, J.; Kastaniotis, A.; Hiltunen, J.; Zhu, Y.
Genetic and biochemical studies in yeast reveal that the cotton fibre-specific GhCER6 gene functions in fatty acid elongation
J. Exp. Bot.
58
473-481
2007
Gossypium hirsutum (Q2QCW7), Gossypium hirsutum
brenda
Tresch, S.; Heilmann, M.; Christiansen, N.; Looser, R.; Grossmann, K.
Inhibition of saturated very-long-chain fatty acid biosynthesis by mefluidide and perfluidone, selective inhibitors of 3-ketoacyl-CoA synthases
Phytochemistry
76
162-171
2012
Arabidopsis thaliana, Lemna aequinoctialis
brenda
Millar, A.; Clemens, S.; Zachgo, S.; Michael Giblin, E.; Taylor, D.; Kunst, L.
CUT1, an Arabidopsis gene required for cuticular wax biosynthesis and pollen fertility, encodes a very-long-chain fatty acid condensing enzyme
Plant Cell
11
825-838
1999
Arabidopsis thaliana
brenda
Fiebig, A.; Mayfield, J.; Miley, N.; Chau, S.; Fischer, R.; Preuss, D.
Alterations in CER6, a gene identical to CUT1, differentially affect long-chain lipid content on the surface of pollen and stems
Plant Cell
12
2001-2008
2000
Arabidopsis thaliana (Q9XF43)
brenda
Reina-Pinto, J.; Voisin, D.; Kurdyukov, S.; Faust, A.; Haslam, R.; Michaelson, L.; Efremova, N.; Franke, B.; Schreiber, L.; Napier, J.; Yephremov, A.
Misexpression of fatty acid elongation1 in the Arabidopsis epidermis induces cell death and suggests a critical role for phospholipase A2 in this process
Plant Cell
21
1252-1272
2009
Arabidopsis thaliana
brenda
Millar, A.; Kunst, L.
Very-long-chain fatty acid biosynthesis is controlled through the expression and specificity of the condensing enzyme
Plant J.
12
121-131
1997
Arabidopsis thaliana
brenda
Todd, J.; Post-Beittenmiller, D.; Jaworski, J.
KCS1 encodes a fatty acid elongase 3-ketoacyl-CoA synthase affecting wax biosynthesis in Arabidopsis thaliana
Plant J.
17
119-130
1999
Arabidopsis thaliana
brenda
Lee, S.; Jung, S.; Go, Y.; Kim, H.; Kim, J.; Cho, H.; Park, O.; Suh, M.
Two Arabidopsis 3-ketoacyl CoA synthase genes, KCS20 and KCS2/DAISY, are functionally redundant in cuticular wax and root suberin biosynthesis, but differentially controlled by osmotic stress
Plant J.
60
462-475
2009
Arabidopsis thaliana
brenda
Purdy, J.G.; Shenk, T.; Rabinowitz, J.D.
Fatty acid elongase 7 catalyzes lipidome remodeling essential for human cytomegalovirus replication
Cell Rep.
10
1375-1385
2015
Homo sapiens (A1L3X0), Homo sapiens
brenda
Sassa, T.; Ohno, Y.; Suzuki, S.; Nomura, T.; Nishioka, C.; Kashiwagi, T.; Hirayama, T.; Akiyama, M.; Taguchi, R.; Shimizu, H.; Itohara, S.; Kihara, A.
Impaired epidermal permeability barrier in mice lacking elovl1, the gene responsible for very-long-chain fatty acid production
Mol. Cell. Biol.
33
2787-2796
2013
Mus musculus
brenda
Tsuda, K.; Akiba, T.; Kimura, F.; Ishibashi, M.; Moriya, C.; Nakagawa, K.; Kurata, N.; Ito, Y.
ONION2 fatty acid elongase is required for shoot development in rice
Plant Cell Physiol.
54
209-217
2013
Oryza sativa
brenda
Haslam, T.M.; Haslam, R.; Thoraval, D.; Pascal, S.; Delude, C.; Domergue, F.; Fernandez, A.M.; Beaudoin, F.; Napier, J.A.; Kunst, L.; Joubes, J.
ECERIFERUM2-LIKE proteins have unique biochemical and physiological functions in very-long-chain fatty acid elongation
Plant Physiol.
167
682-692
2015
Arabidopsis thaliana (Q9SVM9), Arabidopsis thaliana (Q9LIS1)
brenda
Yamauchi, T.; Shiono, K.; Nagano, M.; Fukazawa, A.; Ando, M.; Takamure, I.; Mori, H.; Nishizawa, N.K.; Kawai-Yamada, M.; Tsutsumi, N.; Kato, K.; Nakazono, M.
Ethylene biosynthesis is promoted by very-long-chain fatty acids during lysigenous aerenchyma formation in rice roots
Plant Physiol.
169
180-193
2015
Oryza sativa (Q10PV5), Oryza sativa
brenda
Naganuma, T.; Kihara, A.
Two modes of regulation of the fatty acid elongase ELOVL6 by the 3-ketoacyl-CoA reductase KAR in the fatty acid elongation cycle
PLoS ONE
9
e101823
2014
Homo sapiens (Q9H5J4)
brenda
Morais, S.; Mourente, G.; Martinez, A.; Gras, N.; Tocher, D.R.
Docosahexaenoic acid biosynthesis via fatty acyl elongase and DELTA4-desaturase and its modulation by dietary lipid level and fatty acid composition in a marine vertebrate
Biochim. Biophys. Acta
1851
588-597
2015
Solea senegalensis (G8IIS1)
brenda
Li, C.; Haslam, T.M.; Krueger, A.; Schneider, L.M.; Mishina, K.; Samuels, L.; Yang, H.; Kunst, L.; Schaffrath, U.; Nawrath, C.; Chen, G.; Komatsuda, T.; von Wettstein-Knowles, P.
The beta-ketoacyl-CoA synthase HvKCS1, encoded by Cer-zh, plays a key role in synthesis of barley leaf wax and germination of barley powdery mildew
Plant Cell Physiol.
59
806-822
2018
Hordeum vulgare
brenda
Wang, X.; Guan, Y.; Zhang, D.; Dong, X.; Tian, L.; Qu, L.Q.
A beta-ketoacyl-CoA synthase is involved in rice leaf cuticular wax synthesis and requires a CER2-LIKE protein as a cofactor
Plant Physiol.
173
944-955
2017
Oryza sativa Japonica Group (Q10PV5)
brenda
Yang, Z.; Yang, X.; Dong, S.; Ge, Y.; Zhang, X.; Zhao, X.; Han, N.
Overexpression of beta-ketoacyl-CoA synthase from Vitis vinifera L. improves salt tolerance in Arabidopsis thaliana
Front. Plant Sci.
11
564385
2020
Arabidopsis thaliana (O48780), Vitis vinifera
brenda
Yang, S.; Tang, H.; Wei, X.; Zhao, Y.; Wang, Z.; Su, H.; Niu, L.; Yuan, Y.; Zhang, X.
BrWAX3, encoding a beta-ketoacyl-CoA synthase, plays an essential role in cuticular wax biosynthesis in Chinese cabbage
Int. J. Mol. Sci.
23
10938
2022
Brassica rapa subsp. oleifera (M4E7J4)
brenda
Wang, Y.; Liu, Y.; Pan, X.; Wan, Y.; Li, Z.; Xie, Z.; Hu, T.; Yang, P.
A 3-ketoacyl-CoA synthase 10 (KCS10) homologue from alfalfa enhances drought tolerance by regulating cuticular wax biosynthesis
J. Agric. Food Chem.
71
14493-14504
2023
Medicago sativa (A0A5J6NCI0)
brenda
Chen, J.Y.; Mumtaz, A.; Gonzales-Vigil, E.
Evolution and molecular basis of substrate specificity in a 3-ketoacyl-CoA synthase gene cluster from Populus trichocarpa
J. Biol. Chem.
298
102496
2022
Populus trichocarpa
brenda
Wang, Q.; Du, X.; Zhou, Y.; Xie, L.; Bie, S.; Tu, L.; Zhang, N.; Yang, X.; Xiao, S.; Zhang, X.
The beta-ketoacyl-CoA synthase KCS13 regulates the cold response in cotton by modulating lipid and oxylipin biosynthesis
J. Exp. Bot.
71
5615-5630
2020
Gossypium hirsutum (A0A0P0FPA4)
brenda
Huang, H.; Yang, X.; Zheng, M.; Lue, S.; Zhao, H.
Fine-tuning the activities of beta-KETOACYL-COA SYNTHASE 3 (KCS3) and KCS12 in Arabidopsis is essential for maintaining cuticle integrity
J. Exp. Bot.
74
6575-6587
2023
Arabidopsis thaliana (Q9LQP8), Arabidopsis thaliana (Q9SIB2)
brenda
Luo, N.; Wang, Y.; Liu, Y.; Wang, Y.; Guo, Y.; Chen, C.; Gan, Q.; Song, Y.; Fan, Y.; Jin, S.; Ni, Y.
3-ketoacyl-CoA synthase 19 contributes to the biosynthesis of seed lipids and cuticular wax in Arabidopsis and abiotic stress tolerance
Plant Cell Environ.
47
4599-4614
2024
Arabidopsis thaliana (Q9LZ72)
brenda
Zhang, Z.; Gozdzik, J.; Jetter, R.
Characterization of the closely related Arabidopsis thaliana beta-ketoacyl-CoA synthases KCS3, KCS12 and KCS19
Plant J.
119
490-507
2024
Arabidopsis thaliana (Q9LZ72), Arabidopsis thaliana (Q9LQP8), Arabidopsis thaliana (Q9SIB2)
brenda
Yang, T.; Li, Y.; Liu, Y.; He, L.; Liu, A.; Wen, J.; Mysore, K.S.; Tadege, M.; Chen, J.
The 3-ketoacyl-CoA synthase WFL is involved in lateral organ development and cuticular wax synthesis in Medicago truncatula
Plant Mol. Biol.
105
193-204
2021
Medicago truncatula
brenda
Li, L.; Liang, C.; Zhang, W.; Zhang, X.; Yu, H.; Liu, X.; Bi, Q.; Wang, L.
3-ketoacyl-CoA synthase 7 from Xanthoceras sorbifolium seeds is a crucial regulatory enzyme for nervonic acid biosynthesis
Plant Sci.
347
112184
2024
Xanthoceras sorbifolium
brenda
Li, Z.; Ma, S.; Song, H.; Yang, Z.; Zhao, C.; Taylor, D.; Zhang, M.
A 3-ketoacyl-CoA synthase 11 (KCS11) homolog from Malania oleifera synthesizes nervonic acid in plants rich in 11Z-eicosenoic acid
Tree Physiol.
41
331-342
2021
Malania oleifera
brenda
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