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Information on EC 2.3.1.199 - very-long-chain 3-oxoacyl-CoA synthase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9XF43
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2.3.1.199 very-long-chain 3-oxoacyl-CoA synthaseIUBMB 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
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Word Map
- 2.3.1.199
-
vlcfas
-
polyunsaturated
- acyl-coas
-
desaturase
-
elovls
-
monounsaturated
- cuticular
- ceramide
-
erucic
-
pufas
- sphingolipids
- stearoyl-coa
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oilseed
-
epicuticular
- adrenoleukodystrophy
-
eicosenoic
-
delta6
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docosapentaenoic
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napins
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vlc-pufas
- leek
- suberins
- medicine
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FAE1
KCS20
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -
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
88414-92-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
oleoyl-CoA + malonyl-CoA
?
-
in contrast to stearic acid-CoA, oleic acid-CoA serves as a less suitable substrate for elongation
-
-
?
oleoyl-CoA + malonyl-CoA
CoA + 3-oxo-eicosenoyl-CoA + 3-oxo-erucoyl-CoA + CO2
-
preferred substrate
3-oxo-eicosenoyl-CoA is the major product
-
?
stearoyl-CoA + malonyl-CoA
CoA + 3-oxo-eicosanoyl-CoA + CO2
-
-
major product
-
?
very-long-chain acyl-CoA + malonyl-CoA
CoA + very-long-chain 3-oxoacyl-CoA + CO2
-
-
-
-
?
arachidoyl-CoA + malonyl-CoA
?
-
25% activity compared to oleoyl-CoA
-
-
?
stearoyl-CoA + malonyl-CoA
?
-
best substrate for At2g26640 and FAE1
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
CoA, NADPH and ATP have no effect on the condensation activity of the recombinant enzyme
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
isoform KCS20 and KCS2/DAISY transcripts are approximately 4 and 2fold higher in epidermal peels than in stem
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the enzyme plays a role in the production of epicuticular and pollen coat lipids more than 28 carbons long
malfunction
physiological function
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
-
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
-
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
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 CUT1 enzyme is required for cuticular wax biosynthesis and pollen fertility
physiological function
-
the enzyme is required for epicuticular wax in bolting stems
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
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). KCS6_ARATH
497
2
56396
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the His6-tagged enzyme is purified by Ni2+-pentadentate chelator affinity matrix column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
light is required for expression and expression is increased by salt and drought treatments
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Blacklock, B.; Jaworski, J.
Substrate specificity of Arabidopsis 3-ketoacyl-CoA synthases
Biochem. Biophys. Res. Commun.
346
583-590
2006
Arabidopsis thaliana
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
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
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
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
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)
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
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
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
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
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 (Q9LIS1), Arabidopsis thaliana (Q9SVM9)
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