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Enzyme Nomenclature
Information on EC 2.3.1.75 - long-chain-alcohol O-fatty-acyltransferase
for references in articles please use BRENDA:EC2.3.1.75
Word Map on EC 2.3.1.75
- 2.3.1.75
- acyl-coas
- triacylglycerols
- jojoba
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dgats
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biodiesels
- chinensis
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lubricant
- marinobacter
-
simmondsia
-
monoesters
- aquaeolei
- analysis
- faees
- hexadecanol
- monoacylglycerols
- synthesis
-
oleyl
- baylyi
- agriculture
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
2.3.1.75
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RECOMMENDED NAME
GeneOntology No.
long-chain-alcohol O-fatty-acyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + a long-chain alcohol = CoA + a long-chain ester
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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acyl-CoA + a long-chain alcohol = CoA + a long-chain ester
reaction mechanism
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acyl-CoA + a long-chain alcohol = CoA + a long-chain ester
the catalytic domain contains the highly conserved HHXXXDG motif
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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.
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CAS REGISTRY NUMBER
COMMENTARY
64060-40-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a marine hydrocarbonoclastic bacterium, strain SK2 and several mutant strains, overview, genes atfA1, ABO_2742 and atfA2, ABO_1804, encoding isozymes AtfA1 and AtfA2
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bifunctional wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase, EC 2.3.1.75 and EC 2.3.1.20 resp.
Swissprot
bifunctional wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase, EC 2.3.1.75 and EC 2.3.1.20 resp., enzyme also has acyl-CoA:monoacylglycerol acyltransferase activity, expression in Escherichia coli
Swissprot
bifunctional wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase, EC 2.3.1.75 and EC 2.3.1.20 resp., expression in Escherichia coli and Saccharomyces cerevisiae
Swissprot
bifunctional wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase, EC 2.3.1.75 and EC 2.3.1.20 resp., expression in Escherichia coli with His-tag
Swissprot
wax synthase 10, possibly a pseudogene, no expression in tissues; ecotype Columbia
UniProt
wax synthase 11, possibly a pseudogene, no expression in tissues; ecotype Columbia
UniProt
wax synthase 9, possibly a pseudogene, no expression in tissues; ecotype Columbia
UniProt
AWAT1, i.e. DGA2; X-linked gene AWAT1/DGA2; gene DGAT2L3; isozyme DGA2 or AWAT1
SwissProt
AWAT2, i.e. DC4; X-linked genes AWAT1/DGA2 and AWAT2/DC4; gene DGAT2L4; isozyme DC4 or AWAT2
Swissprot
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
wax synthase gene homologues might play a specialized role in reproductive organs; wax synthase gene homologues might play a specialized role in reproductive organs; wax synthase gene homologues might play a specialized role in reproductive organs; wax synthase gene homologues might play a specialized role in reproductive organs; wax synthase gene homologues might play a specialized role in reproductive organs; wax synthase gene homologues might play a specialized role in reproductive organs; wax synthase gene homologues might play a specialized role in reproductive organs; wax synthase gene homologues might play a specialized role in reproductive organs; wax synthase gene homologues might play a specialized role in reproductive organs; wax synthase gene homologues might play a specialized role in reproductive organs; wax synthase gene homologues might play a specialized role in reproductive organs
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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
1,8-octanedithiol + palmitoyl-CoA
1-S-monopalmitoyloctanedithiol + CoA
59.3% the rate of hexadecanol, plus minor amounts of 1,8-dipalmitoyloctanedithiol
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?
1-decanol + palmitoyl-CoA
decyl palmitate + CoA
48% the rate of hexacedanol
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?
1-hexadecanethiol + palmitoyl-CoA
palmitic acid hexadecane thio ester
10.4% the rate of hexanol
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?
1-S-monopalmitoyloctanedithiol + palmitoyl-CoA
1,8-dipalmitoyloctanedithiol + CoA
13.4% the rate of hexanol
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?
2 1,8-octanedithiol + 3 palmitoyl-CoA
1-S-monopalmitoyloctanedithiol + 1,8-S-dipalmitoyloctanedithiol + 3 CoA
2-cyclohexylethanol + palmitoyl-CoA
2-cyclohexylethyl palmitate + CoA
44.8% the rate of hexacedanol
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?
2-decanol + palmitoyl-CoA
dec-2-yl palmitate + CoA
38.8% the rate of hexacedanol
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?
4-decanol + palmitoyl-CoA
4-decyl palmitate + CoA
15.6% the rate of hexacedanol
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?
cyclododecanol + palmitoyl-CoA
cyclododecyl palmitate + CoA
79.7% the rate of hexacedanol
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?
cyclohexandiol + palmitoyl-CoA
? + CoA
4.1% the rate of hexacedanol
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?
cyclohexanol + palmitoyl-CoA
cyclohexyl palmitate + CoA
32% the rate of hexacedanol
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?
cyclohexanone oxime + palmitoyl-CoA
? + CoA
5.2% the rate of hexacedanol
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?
decanol + palmitoyl-CoA
decanyl palmitate + CoA
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and undecanol, best substrates
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?
eicosanoyl-CoA + cis-11-eicosenol
cis-11-eicosenyl eicosanoate + CoA
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cis-11-eicosenol is the best acceptor
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?
eicosanoyl-CoA + cis-13-eicosenol
cis-13-eicosenyl eicosanoate + CoA
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?
eicosanoyl-CoA + cis-9-octadecenol
cis-9-octadecenyl eicosanoate + CoA
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?
eicosanoyl-CoA + docosanol
docosanyl eicosanoate + CoA
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low activity
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?
eicosanoyl-CoA + eicosanol
eicosanyl eicosanoate + CoA
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low activity
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?
eicosanoyl-CoA + octadecanol
octadecanyl eicosanoate + CoA
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low activity
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?
eicosenoyl-CoA + octadecenol
octadecenyl eicosenoate + CoA
best substrates
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?
hexadecanol + palmitoyl-CoA
hexadecyl palmitate + CoA
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?
oleoyl-CoA + (9Z)-hexadec-9-en-1-ol
CoA + (9Z)-hexadec-9-en-1-yl (9Z)-octadec-9-enoate
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oleoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 1,2-dipalmitoyl-3-oleoyl-sn-glycerol
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palmitoleoyl-CoA + cetyl alcohol
CoA + cetyl palmitoleate
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palmitoleyl alcohol + oleoyl-CoA
CoA + palmitoleyl oleate
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?
palmitoleyl-CoA + myristic acid
palmitoleyl myristate + CoA
enzyme shows preference towards myristic acid and palmitoleyl-CoA
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?
palmitoyl-CoA + butanol
butyl palmitate + CoA
50% of the rate with decanol
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?
palmitoyl-CoA + cetyl alcohol
CoA + cetyl palmitate
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palmitoyl-CoA + decanol
decyl palmitate + CoA
best substrate
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?
palmitoyl-CoA + ethanol
ethyl palmitate + CoA
24% of the rate with decanol
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?
palmitoyl-CoA + hexadecanol
hexadecyl palmitate + CoA
79% of the rate with decanol
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?
palmitoyl-CoA + hexanol
hexyl palmitate + CoA
87% of the rate with decanol
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?
palmitoyl-CoA + isoamyl alcohol
isoamyl palmitate + CoA
57% of the rate with decanol
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?
palmitoyl-CoA + long-chain fatty alcohol
CoA + long-chain palmitoyl ester
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palmitoyl-CoA + octanol
octyl palmitate + CoA
79% of the rate with decanol
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?
phenol + palmitoyl-CoA
phenyl palmitate + CoA
4.1% the rate of hexacedanol
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?
phenylethanol + palmitoyl-CoA
phenylethyl palmitate + CoA
99% the rate of hexacedanol
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?
1-hexadecanethiol + palmitoyl-CoA
palmitic acid hexadecyl thio ester + CoA
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?
1-hexadecanethiol + palmitoyl-CoA
palmitic acid hexadecyl thio ester + CoA
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mutant strain ADP1acr1omegaKm
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?
1-hexadecanol + palmitoyl-CoA
palmitic acid hexadecyl ester + CoA
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best substrate
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?
1-hexadecanol + palmitoyl-CoA
palmitic acid hexadecyl ester + CoA
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mutant strain ADP1acr1omegaKm
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?
1-S-monopalmitoyloctanedithiol + palmitoyl-CoA
1,8-S-dipalmitoyloctanedithiol + CoA
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?
1-S-monopalmitoyloctanedithiol + palmitoyl-CoA
1,8-S-dipalmitoyloctanedithiol + CoA
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mutant strain ADP1acr1omegaKm
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?
2 1,8-octanedithiol + 3 palmitoyl-CoA
1-S-monopalmitoyloctanedithiol + 1,8-S-dipalmitoyloctanedithiol + 3 CoA
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1-S-monopalmitoyloctanedithiol is the main product
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?
2 1,8-octanedithiol + 3 palmitoyl-CoA
1-S-monopalmitoyloctanedithiol + 1,8-S-dipalmitoyloctanedithiol + 3 CoA
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mutant strain ADP1acr1omegaKm
1-S-monopalmitoyloctanedithiol is the main product
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?
2-phenylethanol + palmitoyl-CoA
2-phenylethyl palmitate + CoA
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?
2-phenylethanol + palmitoyl-CoA
2-phenylethyl palmitate + CoA
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?
acyl-CoA + long-chain diacylglycerol
CoA + long-chain triacylglycerol
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acyl-CoA + long-chain diacylglycerol
CoA + long-chain triacylglycerol
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acyl-CoA + long-chain fatty alcohol
CoA + long-chain fatty ester
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acyl-CoA + long-chain fatty alcohol
CoA + long-chain fatty ester
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acyl-CoA + long-chain fatty alcohol
CoA + long-chain fatty ester
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dodecan-1-ol + palmitoyl-CoA
CoA + dodecanyl palmitate
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?
dodecan-1-ol + palmitoyl-CoA
CoA + dodecanyl palmitate
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?
dodecanol + palmitoyl-CoA
dodecanyl palmitate + CoA
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best substrate
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?
dodecanol + palmitoyl-CoA
dodecanyl palmitate + CoA
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and undecanol, best substrates for both isoforms Ma1 and Ma2
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?
dodecanol + palmitoyl-CoA
dodecanyl palmitate + CoA
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?
ethanol + palmitoyl-CoA
ethyl palmitate + CoA
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?
hexadecan-1-ol + palmitoyl-CoA
CoA + hexadecyl palmitate
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?
hexadecan-1-ol + palmitoyl-CoA
CoA + hexadecyl palmitate
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?
hexadecanol + palmitoyl-CoA
hexadecanyl palmitate + CoA
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?
hexadecanol + palmitoyl-CoA
hexadecanyl palmitate + CoA
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?
hexadecanol + palmitoyl-CoA
hexadecanyl palmitate + CoA
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?
hexan-1-ol + palmitoyl-CoA
hexyl palmitate + CoA
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?
hexan-1-ol + palmitoyl-CoA
hexyl palmitate + CoA
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?
isoamyl alcohol + palmitoyl-CoA
isoamyl palmitate + CoA
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?
isoamyl alcohol + palmitoyl-CoA
isoamyl palmitate + CoA
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?
nonan-1-ol + palmitoyl-CoA
CoA + nonyl palmitate
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?
nonan-1-ol + palmitoyl-CoA
CoA + nonyl palmitate
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?
oleoyl-CoA + eicosanol
CoA + icosyl (9Z)-octadec-9-enoate
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oleoyl-CoA + eicosanol
CoA + icosyl (9Z)-octadec-9-enoate
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?
oleoyl-CoA + oleic alcohol
CoA + (9Z)-octadec-9-en-1-yl (9Z)-octadec-9-enoate
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oleoyl-CoA + oleic alcohol
CoA + (9Z)-octadec-9-en-1-yl (9Z)-octadec-9-enoate
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?
palmitoyl-CoA + hexadecanol
CoA + hexadecyl palmitate
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tetradecanol + palmitoyl-CoA
tetradecanyl palmitate + CoA
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best substrate
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?
tetradecanol + palmitoyl-CoA
tetradecanyl palmitate + CoA
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best substrate
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?
undecanol + palmitoyl-CoA
undecanyl palmitate + CoA
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and dodecanol, best substrates for both isoforms Ma1 and Ma2
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?
undecanol + palmitoyl-CoA
undecanyl palmitate + CoA
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and decanol, best substrates
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?
undecanol + palmitoyl-CoA
undecanyl palmitate + CoASH
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?
additional information
?
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key enzyme in the biosynthesis of neutral lipid storage compounds, triacylglycerols and wax esters, overview
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additional information
?
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a bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
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additional information
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WS/DGAT is a very unspecific enzyme and accepts a wide variety of hydrophobic substrates, although also several compounds, e.g. hydroxylamine, sugars, and astaxanthine, do not serve as substrates, substrate specificity, overview. The highly conserved HHXXXDG motif is located at the enzyme's active site, it possesses two histidine residues that are essential for catalysis
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additional information
?
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the order of addition, i.e.the substrate that the protein is incubated with during the first minute while the background absorbance is measured, has a significant impact on the rate of reaction. No substrate: hexanol
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additional information
?
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WS/DGAT is a very unspecific enzyme and accepts a wide variety of hydrophobic substrates, although also several compounds, e.g. hydroxylamine, sugars, and astaxanthine, do not serve as substrates, substrate specificity, overview. The highly conserved HHXXXDG motif is located at the enzyme's active site, it possesses two histidine residues that are essential for catalysis
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additional information
?
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the bifunctional wax ester synthase/acyl coenzyme A (acyl-CoA):diacylglycerol acyltransferase from Acinetobacter sp. strain ADP1 mediates the biosyntheses of wax esters and triacylglycerols
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additional information
?
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the bifunctional enzyme catalyzes the reactions of the diacylglycerol transferase, EC 2.3.1.20, and of the wax synthase, EC 2.3.1.75, substrate specificity of the wax ester synthase activity with alkanethiols as alternative acyl acceptors
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additional information
?
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the enzyme plays the key role in the biosynthesis of triacylglycerols and wax esters, overview
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additional information
?
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acyl acceptor specificities of isozymes AtfA1 and AtfA2 from A. borkumensis SK2 for glycerol and acylglycerols, overview
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additional information
?
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WSD1, a member of the bifunctional wax ester synthase/diacylglycerol acyltransferase gene family, plays a key role in wax ester synthesis in Arabidopsis
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additional information
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the enzyme has a high level of wax synthase activity and approximately 10fold lower level of diacylglycerol acyltransferase activity
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additional information
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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
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the enzyme plays an important role in lipid metabolism in human skin, overview
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additional information
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the multifunctional enzyme plays an important role in lipid metabolism in human skin
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additional information
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the multifunctional enzyme plays an important role in lipid metabolism in human skin
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additional information
?
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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
?
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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
?
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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
?
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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
?
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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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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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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
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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
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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
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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
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additional information
?
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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 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 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 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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additional information
?
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the enzyme is involved in synthesis of isoprenoid wax ester storage compounds, pathway, overview
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additional information
?
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substrate profiles of isozymes WS1 and WS2, acyl-CoA specificity of isozyme WS2 with preference for palmitoyl-CoA and broad activity with alcohols of various chain lengths, bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
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additional information
?
-
-
the order of addition, i.e.the substrate that the protein is incubated with during the first minute while the background absorbance is measured, has a significant impact on the rate of reaction. No substrate: hexanol
-
-
-
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
-
-
-
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
-
-
-
additional information
?
-
-
DGAT1 is catalyzing the reactions of the monoacylglycerol transferase, EC 2.3.1.22, of the diacylglycerol transferase, EC 2.3.1.20, of the wax synthase, EC 2.3.1.75, and of the acyl-CoA:retinol acyltransferase, EC 2.3.1.76, DGAT2 catalyzes the wax ester synthase reaction, overview
-
-
-
additional information
?
-
-
the highest activity is observed for 14:0-CoA, 12:0-CoA, and 16:0-CoA in combination with medium chain alcohols (up to 5.2, 3.4, and 3.3 nmol wax esters/min/mg microsomal protein, respectively). Unsaturated alcohols longer than 18C are better utilized by the enzyme in comparison to the saturated ones. Combinations of all tested alcohols with 20:0-CoA, 22:1-CoA, or ricinoleoyl-CoA are poorly utilized by the enzyme, and conjugated acyl-CoAs are not utilized at all
-
-
-
additional information
?
-
-
the order of addition, i.e.the substrate that the protein is incubated with during the first minute while the background absorbance is measured, has a significant impact on the rate of reaction. No substrate: hexanol
-
-
-
additional information
?
-
-
the order of addition, i.e.the substrate that the protein is incubated with during the first minute while the background absorbance is measured, has a significant impact on the rate of reaction. No substrate: hexanol
-
-
-
additional information
?
-
-
eicosanoyl-CoA can be replaced by stearoyl-CoA or cis-11-eicosenoyl-CoA with equal reactivity
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
1-hexadecanethiol + palmitoyl-CoA
palmitic acid hexadecyl thio ester + CoA
-
mutant strain ADP1acr1omegaKm
-
-
?
1-hexadecanol + palmitoyl-CoA
palmitic acid hexadecyl ester + CoA
-
mutant strain ADP1acr1omegaKm
-
-
?
1-S-monopalmitoyloctanedithiol + palmitoyl-CoA
1,8-S-dipalmitoyloctanedithiol + CoA
-
mutant strain ADP1acr1omegaKm
-
-
?
2 1,8-octanedithiol + 3 palmitoyl-CoA
1-S-monopalmitoyloctanedithiol + 1,8-S-dipalmitoyloctanedithiol + 3 CoA
-
mutant strain ADP1acr1omegaKm
1-S-monopalmitoyloctanedithiol is the main product
-
?
acyl-CoA + long-chain diacylglycerol
CoA + long-chain triacylglycerol
Q58HT5, Q6E213, Q6ZPD8
-
-
-
-
acyl-CoA + long-chain fatty alcohol
CoA + long-chain fatty ester
Q58HT5, Q6E213, Q6ZPD8
-
-
-
-
acyl-CoA + long-chain fatty alcohol
CoA + long-chain fatty ester
-
-
-
-
-
additional information
?
-
-
key enzyme in the biosynthesis of neutral lipid storage compounds, triacylglycerols and wax esters, overview
-
-
-
additional information
?
-
-
the bifunctional wax ester synthase/acyl coenzyme A (acyl-CoA):diacylglycerol acyltransferase from Acinetobacter sp. strain ADP1 mediates the biosyntheses of wax esters and triacylglycerols
-
-
-
additional information
?
-
-
the enzyme plays the key role in the biosynthesis of triacylglycerols and wax esters, overview
-
-
-
additional information
?
-
-
WSD1, a member of the bifunctional wax ester synthase/diacylglycerol acyltransferase gene family, plays a key role in wax ester synthesis in Arabidopsis
-
-
-
additional information
?
-
-
the enzyme plays an important role in lipid metabolism in human skin, overview
-
-
-
additional information
?
-
Q6E213
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
?
-
Q6E213
the multifunctional enzyme plays an important role in lipid metabolism in human skin
-
-
-
additional information
?
-
-
the enzyme is involved in synthesis of isoprenoid wax ester storage compounds, pathway, overview
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bovine serum albumin
-
defatted, 2fold activation in crude enzyme extract at concentration below 5 mg/ml, inhibition above
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.4
hexan-1-ol
-
wild-type, temperature not specified in the publication, pH not specified in the publication
5.6
isoamyl alcohol
-
wild-type, temperature not specified in the publication, pH not specified in the publication
additional information
additional information
-
kinetics of isozymes WS1 and WS2
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.08
1.6
-
substrate hexadecan-1-ol, mutant A360I, pH not specified in the publication, temperature not specified in the publication
1.64
-
substrate hexadecan-1-ol, mutant A360V, pH not specified in the publication, temperature not specified in the publication
1.85
-
substrate hexadecan-1-ol, mutant A360F, pH not specified in the publication, temperature not specified in the publication
2.7
-
substrate hexadecan-1-ol, wild-type, pH not specified in the publication, temperature not specified in the publication
3.6
-
substrate nonan-1-ol, wild-type, pH not specified in the publication, temperature not specified in the publication
7.8
-
substrate nonan-1-ol, mutant A360F, pH not specified in the publication, temperature not specified in the publication
16.6
-
substrate nonan-1-ol, mutant A360V, pH not specified in the publication, temperature not specified in the publication
19.6
-
substrate nonan-1-ol, mutant A360I, pH not specified in the publication, temperature not specified in the publication
34.3
-
substrate dodecan-1-ol, mutant A360I, pH not specified in the publication, temperature not specified in the publication
34.6
-
substrate dodecan-1-ol, mutant A360F, pH not specified in the publication, temperature not specified in the publication
35.9
-
substrate dodecan-1-ol, mutant A360V, pH not specified in the publication, temperature not specified in the publication
46.5
-
substrate dodecan-1-ol, wild-type, pH not specified in the publication, temperature not specified in the publication
70
Q8GG1
substrate hexadecan-1-ol, wild-type, pH not specified in the publication, temperature not specified in the publication
80
Q8GG1
substrate hexadecan-1-ol, mutant G355I, pH not specified in the publication, temperature not specified in the publication
140
Q8GG1
substrate nonan-1-ol, wild-type, pH not specified in the publication, temperature not specified in the publication
360
Q8GG1
substrate nonan-1-ol, mutant G355I, pH not specified in the publication, temperature not specified in the publication
960
Q8GG1
substrate dodecan-1-ol, wild-type, pH not specified in the publication, temperature not specified in the publication
1700
Q8GG1
substrate dodecan-1-ol, mutant G355I, pH not specified in the publication, temperature not specified in the publication
additional information
additional information
-
fatty acid content and fatty acid composition of Alcanivorax borkumensis strains and fatty acid composition of purified lipids isolated from strain SK2, overview
additional information
-
substrate specificity, overview; substrate specificity, overview
additional information
substrate specificity, overview; substrate specificity, overview
additional information
substrate specificity, overview; substrate specificity, overview
additional information
substrate specificity, overview; substrate specificity, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.05
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
-
cells grown on phytol as the sole carbon source under limiting nitrogen and/or phosphorous conditions
-
;
-
additional information
predominant expression; predominant expression; predominant expression; predominant expression of AWAT1; predominant expression of AWAT2
-
additional information
-
tissue distribution of DC3 expression, overview; tissue distribution of DC4 expression, overview; tissue distribution of DGA2 expression, overview
additional information
tissue distribution of DC3 expression, overview; tissue distribution of DC4 expression, overview; tissue distribution of DGA2 expression, overview
additional information
tissue distribution of DC3 expression, overview; tissue distribution of DC4 expression, overview; tissue distribution of DGA2 expression, overview
additional information
tissue distribution of DC3 expression, overview; tissue distribution of DC4 expression, overview; tissue distribution of DGA2 expression, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is located mainly on the membrane's cytosolic site and on the surface of intracellular wax ester inclusions, it possesses one putative predicted membrane-spanning region in hydrophobicity analysis
additional information
-
the enzyme exhibits a very specific adsorption pattern to artificial phospholipid membranes
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
38536
-
x * 38599, AWAT1, sequence calculation, x * 38536, AWAT2, sequence calculation
38599
-
x * 38599, AWAT1, sequence calculation, x * 38536, AWAT2, sequence calculation
51800
additional information
amino acid sequence analysis and alignment
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 37759, AWAT1, sequence calculation; x * 38094, AWAT2, sequence calculation
?
-
x * 38599, AWAT1, sequence calculation, x * 38536, AWAT2, sequence calculation
?
x * 37573, AWAT1, sequence calculation; x * 38145, AWAT2, sequence calculation
additional information
-
the enzyme contains the highly conserved HHXXXDG motif, amino acids 133-138, which may be involved in fatty acyl-CoA binding or catalytically participate in the acyltransferase reaction
additional information
predicted secondary and transmembrane structures of isozyme AWAT1, overview; predicted secondary and transmembrane structures of isozyme AWAT2, overview
additional information
predicted secondary and transmembrane structures of isozyme AWAT1, overview; predicted secondary and transmembrane structures of isozyme AWAT2, overview
additional information
-
predicted secondary and transmembrane structures of isozymes AWAT1 and AWAT2, overview
additional information
predicted secondary and transmembrane structures of isozyme AWAT1, overview; predicted secondary and transmembrane structures of isozyme AWAT2, overview
additional information
predicted secondary and transmembrane structures of isozyme AWAT1, overview; predicted secondary and transmembrane structures of isozyme AWAT2, overview
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
no improvement of heat-stability by polyvinylpyrrolidone
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
decrease in activity with buffers such as Tris, Bis-Tris, HEPES, morpholinoethanesulfonic acid
highly sensitive to proteases, especially to metallorpoteases, proteolysis is inhibited by addition of a cocktail of protease inhibitors including EDTA
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli by cation exchange chromatography, hydrophobic interaction chromatography and subsequent anion exchange chromatography or by means of a C-terminal His6 tag
-
recombinant soluble N-terminally His-tagged enzyme 19.2fold from Escherichia coli strain BL21(DE3) by cation exchange and nickel affinity chromatography
-
recombinant wild-type and mutant enzymes from Escherichia coli by cation exchange and hydrophobic interaction chromatography, followed by anion exchange chromatography
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chromosomal location, expression of the FLAG-tagged enzyme in Spodoptera frugiperda Sf9 cells and in COS-7 cells; 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
cloning of cDNA, DNA sequence analysis, construction of plasmid to express the cDNA in transgenic Arabidopsis thaliana plants
delta integration in Saccharomyces cerevisiae, resulting in 1–6 copies of the integration construct per genome
DNA and amino acid sequence determination and analysis of wax synthase analogous genes, expression patterns, overview; DNA and amino acid sequence determination and analysis of wax synthase analogous genes, expression patterns, overview; DNA and amino acid sequence determination and analysis of wax synthase analogous genes, expression patterns, overview; DNA and amino acid sequence determination and analysis of wax synthase analogous genes, expression patterns, overview; DNA and amino acid sequence determination and analysis of wax synthase analogous genes, expression patterns, overview; DNA and amino acid sequence determination and analysis of wax synthase analogous genes, expression patterns, overview; DNA and amino acid sequence determination and analysis of wax synthase analogous genes, expression patterns, overview; DNA and amino acid sequence determination and analysis of wax synthase analogous genes, expression patterns, overview; DNA and amino acid sequence determination and analysis of wax synthase analogous genes, expression patterns, overview; DNA and amino acid sequence determination and analysis of wax synthase analogous genes, expression patterns, overview; DNA and amino acid sequence determination and analysis of wax synthase analogous genes, expression patterns, overview
expression as soluble N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli
expression in Saccharomyces cerevisiae
gene atfA, DNA and amino acid sequence determination and analysis, WS/DGAT family sequence comparisons and phylogenetic relationships, overview, expression in Escherichia coli as untagged or C-terminally His6-tagged enzyme
-
gene atfA, expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta(DE3)
-
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
genes atfA1 and atfA2, expression in Escherichia coli strain BL21(DE3)
-
genes with high homologies to the Acinetobacter sp. ADP1 atfA are identified in the genome databases of several Gram-negative strains, including marine bacteria like Hahella chejuensis, psychrophilic strains like Psychrobacter sp., Polaromonas sp. and Bradyrhizobium japonicum. Ten atfA homologous genes are identified in the genome database of Arabidopsis thaliana
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
isozymes AWAT1 and AWAT2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
-
screening, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM109
-
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
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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D137A
-
the mutant shows slightly reduced activity compared to the wild-type enzyme
G138A
-
the mutant shows slightly reduced activity compared to the wild-type enzyme
H133L
-
the replacement of His133 leads to highly reduced enzyme activity
A360F
-
mutation slightly improves the rate of reaction found for smaller fatty alcohols
A360I
-
mutation improves the rate of reaction found for smaller fatty alcohols
A360V
-
mutation improves the rate of reaction found for smaller fatty alcohols
L356F
-
mutation increases selectivity toward ethanol, with a drop in specific activity of approximately 89% for dodecanol
L356V
-
mutation increases selectivity toward 2-phenylethanol
M405A
-
significant decrease in overall activity with dodecanol
M405F
-
mutation increases selectivity toward isoamyl alcohol, significant decrease in overall activity with dodecanol
M405L
-
significant decrease in overall activity with dodecanol
M405W
-
dramatically shifts selectivity toward ethanol, significant decrease in overall activity with dodecanol
A360F
-
mutation slightly improves the rate of reaction found for smaller fatty alcohols
-
A360I
-
mutation improves the rate of reaction found for smaller fatty alcohols
-
A360V
-
mutation improves the rate of reaction found for smaller fatty alcohols
-
L356A
-
mutation increases selectivity toward ethanol
-
L356F
-
mutation increases selectivity toward ethanol, with a drop in specific activity of approximately 89% for dodecanol
-
L356V
-
mutation increases selectivity toward 2-phenylethanol
-
M405F
-
mutation increases selectivity toward isoamyl alcohol, significant decrease in overall activity with dodecanol
-
N36R
-
mutant enzyme is capable of synthesizing very long chain fatty acyl-harboring wax esters
additional information
additional information
-
establishment of heterologous wax ester biosynthesis in a recombinant Escherichia coli strain by coexpression of a fatty alcohol-producing bifunctional acyl-coenzyme A reductase from the jojoba plant, Simmondsia chinensis, and a bacterial wax ester synthase from Acinetobacter baylyi strain ADP1, catalyzing the esterification of fatty alcohols and coenzyme A thioesters of fatty acids, succesful production of jojoba oil-like wax esters, such as palmityl oleate, palmityl palmitoleate, and oleyl oleate, in presence of oleate, but also of fatty acid butyl esters, overview
additional information
-
construction of knockout mutants by transposon mutagenesis
additional information
-
establishment of heterologous wax ester biosynthesis in a recombinant Escherichia coli strain by coexpression of a fatty alcohol-producing bifunctional acyl-coenzyme A reductase from the jojoba plant, Simmondsia chinensis, and a bacterial wax ester synthase from Acinetobacter baylyi strain ADP1, catalyzing the esterification of fatty alcohols and coenzyme A thioesters of fatty acids, succesful production of jojoba oil-like wax esters, such as palmityl oleate, palmityl palmitoleate, and oleyl oleate, in presence of oleate, but also of fatty acid butyl esters, overview
-
additional information
-
the knockout mutant Acinetobacter sp. strain ADP1acr1omegaKm is unable to produce fatty alcohols
additional information
co-expression of fatty acyl-CoA reductase and wax synthase in Saccharomyces cerevisiae results in synthesis of myristyl myristate, myristyl palmitoleate, myristyl palmitate and palmityl myristate when fed with myristic acid
additional information
-
the wax diester synthase activity of DGAT1 helps to explain the deficiency of type II wax diesters in the fur lipids of Dgat-/- mice
additional information
-
domain swap experiment between the mouse acyl-CoA:wax alcohol acyltransferase (AWAT2) and the homologous mouse acyl-CoA:diacylglycerol O-acyltransferase 2 (DGAT2). Te substrate specificity of AWAT2 is partially determined by two predicted transmembrane domains near the amino terminus of AWAT2. Upon exchange of the two domains for the respective part of DGAT2, the resulting chimeric enzyme is capable of incorporating up to 20% of very long acyl chains in the wax esters upon expression in Saccharomyces cerevisiae. The amount of very long acyl chains in wax esters synthesized by wild type AWAT2 is negligible. The effect is due to a single amino acid exchange within one of the predicted membrane domains, the AWAT2 N36R
additional information
cloned cDNA is expressed in transgenic Arabidopsis thaliana plants, in combination with cDNAs encoding the jojoba fatty acyl-CoA reductase and a beta-ketoacyl-CoA synthase from Lunaria annua under a seed specific promotor, highly enhanced wax content in transgenic seeds
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
transgenic plants expressing the enzyme allow the production of long-chain liquid waxes at reasonable cost for use in commercial applications
analysis
synthesis
analysis
-
development of an enzymic assay by indirect measurement of fatty alcohol and fatty acyl-CoA esterification catalyzed by the WS/DGAT enzyme using the coupled reaction of 5,5'-dithiobis(2-nitrobenzoic acid) with free CoA liberated during the esterification reaction
analysis
-
development of an enzymic assay by indirect measurement of fatty alcohol and fatty acyl-CoA esterification catalyzed by the WS/DGAT enzyme using the coupled reaction of 5,5'-dithiobis(2-nitrobenzoic acid) with free CoA liberated during the esterification reaction
analysis
-
development of an enzymic assay by indirect measurement of fatty alcohol and fatty acyl-CoA esterification catalyzed by the WS/DGAT enzyme using the coupled reaction of 5,5'-dithiobis(2-nitrobenzoic acid) with free CoA liberated during the esterification reaction
analysis
-
development of an enzymic assay by indirect measurement of fatty alcohol and fatty acyl-CoA esterification catalyzed by the WS/DGAT enzyme using the coupled reaction of 5,5'-dithiobis(2-nitrobenzoic acid) with free CoA liberated during the esterification reaction
analysis
-
development of an enzymic assay by indirect measurement of fatty alcohol and fatty acyl-CoA esterification catalyzed by the WS/DGAT enzyme using the coupled reaction of 5,5'-dithiobis(2-nitrobenzoic acid) with free CoA liberated during the esterification reaction
-
synthesis
synthesis of fatty acid ethyl esters in Saccharomyces cerevisiae by gene integration into chromosomal delta sequences using repetitive transformation, which results in 1-6 copies of the integration construct per genome. The corresponding fatty acid ethyl ester production increases up to 34 mg/L, an about sixfold increase compared to the equivalent plasmid-based producer. The cassette in the yeast genome is stably maintained in nonselective medium after deletion of RAD52. Additional overexprerssion of genes encoding endogenous acyl-CoA binding protein and a bacterial NADP+-dependent glyceraldehyde-3-phosphate dehydrogenase (gapN) leads to another 40% increase in fatty acid ethyl ester production
synthesis
-
expression of a fusion protein between Marinobacter hydrocarbonoclasticus wax synthase and Marinobacter adhaerens fatty acyl-CoA reductase in Nicotiana benthaminana. Compared to wild-type controls, transgenic plants show both in leaves and stems a significant increase in the total level of wax esters, being eight-fold at the whole plant level. The profiles of fatty acid methyl ester and fatty alcohol in wax esters are related, and C16 and C18 molecules constitute predominant forms. Strong transformants display certain developmental aberrations, such as stunted growth and chlorotic leaves and stems. These negative effects are associated with an accumulation of fatty alcohols
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.75)
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