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Information on EC 2.3.1.75 - long-chain-alcohol O-fatty-acyltransferase and Organism(s) Homo sapiens
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EC Tree
2.3.1.75 long-chain-alcohol O-fatty-acyltransferaseIUBMB Comments
Transfers saturated or unsaturated acyl residues of chain-length C18 to C20 to long-chain alcohols, forming waxes. The best acceptor is cis-icos-11-en-1-ol.
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Word Map
- 2.3.1.75
- acyl-coas
- esterification
-
retinyl
-
arats
-
biodiesels
-
lubricant
- marinobacter
- jojoba
-
retinol-binding
-
3hretinol
-
lecithin:retinol
-
simmondsia
- faees
- aquaeolei
- synthesis
- baylyi
-
acyl-coa-dependent
- hexadecanol
- analysis
- agriculture
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
acyl-coa:retinol acyltransferase, wax synthase, wax ester synthase, awat2, awat1, atfa1, wax ester synthase/diacylglycerol acyltransferase, maqu_0168, wax ester synthase/acyl-coenzyme a:diacylglycerol acyltransferase, acyl-coa wax alcohol acyltransferases, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyltransferase, long-chain alcohol
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-
-
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AWAT2
MFAT
multifunctional O-acyltransferase
wax synthase
wax-ester synthase
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-
additional information
wax synthase
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-
-
additional information
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the enzyme belongs to the acyl-CoA:diacylglycerol acyltransferase 2/acyl-CoA:monoacylglycerol acyltransferase, MGAT, gene family
additional information
cf. EC 2.3.1.20, the enzyme belongs to the acyl-CoA:diacylglycerol acyltransferase, DGAT, 2 gene superfamily
additional information
the enzyme belongs to the diacylglycerol acyltransferase 2, DGAT2, gene superfamily, cf. EC 2.3.1.20
additional information
cf. EC 2.3.1.20 and EC 2.3.1.22, the enzyme belongs to the acyl-CoA:diacylglycerol acyltransferase 2/acyl-CoA:monoacylglycerol acyltransferase, MGAT, gene family
additional information
cf. EC 2.3.1.20, the enzyme belongs to the acyl-CoA:diacylglycerol acyltransferase, DGAT, 2 gene superfamily
additional information
the enzyme belongs to the diacylglycerol acyltransferase 2, DGAT2, gene superfamily, cf. EC 2.3.1.20
additional information
the enzyme belongs to the diacylglycerol acyltransferase 2, DGAT2, gene superfamily, cf. EC 2.3.1.20
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:long-chain-alcohol O-acyltransferase
Transfers saturated or unsaturated acyl residues of chain-length C18 to C20 to long-chain alcohols, forming waxes. The best acceptor is cis-icos-11-en-1-ol.
CAS REGISTRY NUMBER
COMMENTARY
64060-40-8
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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
acyl-CoA + long-chain diacylglycerol
CoA + long-chain triacylglycerol
-
-
-
?
acyl-CoA + long-chain fatty alcohol
CoA + long-chain fatty ester
-
-
-
?
oleoyl-CoA + (9Z)-hexadec-9-en-1-ol
CoA + (9Z)-hexadec-9-en-1-yl (9Z)-octadec-9-enoate
-
-
-
?
oleoyl-CoA + eicosanol
CoA + icosyl (9Z)-octadec-9-enoate
-
-
-
?
oleoyl-CoA + oleic alcohol
CoA + (9Z)-octadec-9-en-1-yl (9Z)-octadec-9-enoate
-
-
-
?
palmitoleoyl-CoA + cetyl alcohol
CoA + cetyl palmitoleate
-
-
-
?
palmitoleyl alcohol + oleoyl-CoA
CoA + palmitoleyl oleate
-
-
-
?
palmitoyl-CoA + cetyl alcohol
CoA + cetyl palmitate
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-
-
?
additional information
?
-
prefers monounsaturated and polyunsaturated C18:1 and C18:2 fatty alcohols over C18:0, and prefers 20:1 fatty alcohol over C20:0. Enzyme prefers shorter chain fatty acyl-CoA substrates and does not discriminate between monounsaturated and polyunsaturated fatty acyl CoA substrates. Enzyme also uses 10, 15, and 20 carbon isoprenoid alcohols
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-
?
additional information
?
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-
the enzyme plays an important role in lipid metabolism in human skin, overview
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-
?
additional information
?
-
the enzyme plays an important role in lipid metabolism in human skin, overview
-
-
?
additional information
?
-
-
the multifunctional enzyme plays an important role in lipid metabolism in human skin
-
-
?
additional information
?
-
the multifunctional enzyme plays an important role in lipid metabolism in human skin
-
-
?
additional information
?
-
AWAT 1 predominantly esterifies long chain, wax alcohols with acyl-CoA-derived fatty acids to produce wax esters, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation, overview
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-
?
additional information
?
-
AWAT 1 predominantly esterifies long chain, wax alcohols with acyl-CoA-derived fatty acids to produce wax esters, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation, overview
-
-
?
additional information
?
-
AWAT 1 predominantly esterifies long chain, wax alcohols with acyl-CoA-derived fatty acids to produce wax esters, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation, overview
-
-
?
additional information
?
-
-
AWAT 1 predominantly esterifies long chain, wax alcohols with acyl-CoA-derived fatty acids to produce wax esters, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation, overview
-
-
?
additional information
?
-
AWAT 2 predominantly esterifies long chain, wax alcohols with acyl-CoA-derived fatty acids to produce wax esters, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation, overview, no activity of AWAT2 with 1-decanol
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-
?
additional information
?
-
AWAT 2 predominantly esterifies long chain, wax alcohols with acyl-CoA-derived fatty acids to produce wax esters, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation, overview, no activity of AWAT2 with 1-decanol
-
-
?
additional information
?
-
AWAT 2 predominantly esterifies long chain, wax alcohols with acyl-CoA-derived fatty acids to produce wax esters, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation, overview, no activity of AWAT2 with 1-decanol
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-
?
additional information
?
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AWAT 2 predominantly esterifies long chain, wax alcohols with acyl-CoA-derived fatty acids to produce wax esters, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation, overview, no activity of AWAT2 with 1-decanol
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?
additional information
?
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bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
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-
?
additional information
?
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bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
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?
additional information
?
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bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
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?
additional information
?
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bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
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?
additional information
?
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substrate specificity of AWAT1, overview, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation and predominantly esterify long chain alcohols with acyl-CoA-derived fatty acids to produce wax esters, bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
-
-
?
additional information
?
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substrate specificity of AWAT1, overview, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation and predominantly esterify long chain alcohols with acyl-CoA-derived fatty acids to produce wax esters, bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
-
-
?
additional information
?
-
substrate specificity of AWAT1, overview, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation and predominantly esterify long chain alcohols with acyl-CoA-derived fatty acids to produce wax esters, bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
-
-
?
additional information
?
-
-
substrate specificity of AWAT1, overview, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation and predominantly esterify long chain alcohols with acyl-CoA-derived fatty acids to produce wax esters, bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
-
-
?
additional information
?
-
substrate specificity of AWAT2, overview, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation and predominantly esterify long chain alcohols with acyl-CoA-derived fatty acids to produce wax esters, bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
-
-
?
additional information
?
-
substrate specificity of AWAT2, overview, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation and predominantly esterify long chain alcohols with acyl-CoA-derived fatty acids to produce wax esters, bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
-
-
?
additional information
?
-
substrate specificity of AWAT2, overview, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation and predominantly esterify long chain alcohols with acyl-CoA-derived fatty acids to produce wax esters, bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
-
-
?
additional information
?
-
-
substrate specificity of AWAT2, overview, AWAT1 and AWAT2 have very distinct substrate preferences in terms of alcohol chain length and fatty acyl saturation and predominantly esterify long chain alcohols with acyl-CoA-derived fatty acids to produce wax esters, bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
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-
?
additional information
?
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substrate specificity, overview, a human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters, overview, the enzyme catalyzes also the reactions of EC 2.3.1.20 and EC 2.3.1.22
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?
additional information
?
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substrate specificity, overview, a human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters, overview, the enzyme catalyzes also the reactions of EC 2.3.1.20 and EC 2.3.1.22
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?
additional information
?
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the multifunctional O-acetyltransferase is catalyzing the reactions of the wax synthase, of the diacylglycerol transferase, EC 2.3.1.20, of the monoacylglycerol transferase, EC 2.3.1.22, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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-
?
additional information
?
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the multifunctional O-acetyltransferase is catalyzing the reactions of the wax synthase, of the diacylglycerol transferase, EC 2.3.1.20, of the monoacylglycerol transferase, EC 2.3.1.22, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, overview
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-
?
NATURAL SUBSTRATE
NATURAL 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
acyl-CoA + long-chain diacylglycerol
CoA + long-chain triacylglycerol
-
-
-
?
acyl-CoA + long-chain fatty alcohol
CoA + long-chain fatty ester
-
-
-
?
additional information
?
-
-
the enzyme plays an important role in lipid metabolism in human skin, overview
-
-
?
additional information
?
-
the enzyme plays an important role in lipid metabolism in human skin, overview
-
-
?
additional information
?
-
-
the multifunctional enzyme plays an important role in lipid metabolism in human skin
-
-
?
additional information
?
-
the multifunctional enzyme plays an important role in lipid metabolism in human skin
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). AWAT1_HUMAN
328
1
37759
Swiss-Prot
Secretory Pathway (Reliability: 1)
AWAT2_HUMAN
333
3
38094
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
predicted secondary and transmembrane structures of isozyme AWAT1, overview
additional information
predicted secondary and transmembrane structures of isozyme AWAT1, overview
additional information
-
predicted secondary and transmembrane structures of isozyme AWAT1, overview
additional information
predicted secondary and transmembrane structures of isozyme AWAT2, overview
additional information
predicted secondary and transmembrane structures of isozyme AWAT2, overview
additional information
-
predicted secondary and transmembrane structures of isozyme AWAT2, overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
chromosomal location, expression of the FLAG-tagged enzyme in Spodoptera frugiperda Sf9 cells and in COS-7 cells
gene AWAT1, i.e. DGA2, location on the X chromosome Xq13.1, DNA and amino acid sequence determination and analysis, expression analysis, expression in Saccharomyces cerevisiae
gene DC3, DNA and amino acid sequence determination and analysis, genetic organization and phylogenetics, expression in Saccharomyces cerevisiae
gene DC4, DNA and amino acid sequence determination and analysis, genetic organization and phylogenetics, expression in Saccharomyces cerevisiae
gene DC4, i.e. AWAT2, location on the X chromosome Xq13.1, DNA and amino acid sequence determination and analysis, expression analysis, expression in Saccharomyces cerevisiae
gene DGAT2, DNA and amino acid sequence determination and analysis, genetic organization and phylogenetics, expression in Saccharomyces cerevisiae
isozyme AWAT1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
isozyme AWAT2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
MFAT, DNA and amino acid sequence determination and analysis, localized on the X chromosome, expression of the N-terminally FLAG-tagged enzyme in Spodoptera frugierda Sf9 cells using the baculovirus transfection system, or in COS-7 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cheng, J.B.; Russell, D.W.
Mammalian wax biosynthesis. II. Expression cloning of wax synthase cDNAs encoding a member of the acyltransferase enzyme family
J. Biol. Chem.
279
37798-37807
2004
Homo sapiens (Q6E213), Mus musculus (Q6E1M8), Mus musculus
Yen, C.L.; Brown Iv, C.H.; Monetti, M.; Farese, R.V., Jr.
A human skin multifunctional O-acyltransferase that catalyzes the synthesis of acylglycerols, waxes, and retinyl esters
J. Lipid Res.
46
2388-2397
2005
Homo sapiens, Homo sapiens (Q6E213)
Turkish, A.R.; Henneberry, A.L.; Cromley, D.; Padamsee, M.; Oelkers, P.; Bazzi, H.; Christiano, A.M.; Billheimer, J.T.; Sturley, S.L.
Identification of two novel human acyl-CoA wax alcohol acyltransferases: members of the diacylglycerol acyltransferase 2 (DGAT2) gene superfamily
J. Biol. Chem.
280
14755-14764
2005
Homo sapiens (Q58HT5), Homo sapiens (Q6E213), Homo sapiens (Q6ZPD8), Homo sapiens
Holmes, R.
Comparative genomics and proteomics of vertebrate diacylglycerol acyltransferase (DGAT), acyl CoA wax alcohol acyltransferase (AWAT) and monoacylglycerol acyltransferase (MGAT)
Comp. Biochem. Physiol. D
5
45-54
2010
Homo sapiens (Q58HT5), Homo sapiens (Q6E213), Homo sapiens, Monodelphis domestica, Mus musculus (A2ADU9), Mus musculus (Q6E1M8), Mus musculus
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