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Information on EC 2.3.1.75 - long-chain-alcohol O-fatty-acyltransferase
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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
- jojoba
- marinobacter
-
biodiesels
- faees
-
lubricant
-
retinol-binding
-
lecithin:retinol
-
simmondsia
-
3hretinol
- aquaeolei
-
acyl-coa-dependent
- analysis
- hexadecanol
- synthesis
- agriculture
The enzyme appears in viruses and cellular organisms
Synonyms
acyl-coa:retinol acyltransferase, wax synthase, wax ester synthase, awat2, wax ester synthase/diacylglycerol acyltransferase, atfa1, awat1, maqu_0168, wax ester synthase/acyl-coenzyme a:diacylglycerol acyltransferase, egwsd2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyl CoA wax alcohol acyltransferase 1
acyl CoA wax alcohol acyltransferase 2
acyl-CoA wax alcohol acyltransferase 2
ATF
ATF1
AtfA
AWAT1
AWAT2
Maqu_0168
MFAT
multifunctional O-acyltransferase
unspecific bifunctional wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase
wax ester synthase
wax ester synthase/acyl-CoA diacylglycerol acyltransferase
-
wax ester synthase/acyl-CoA:diacylglycerol acyltransferase
wax ester synthase/acyl-coenzyme A:diacylglycerol acyltransferase
-
-
wax ester synthase/diacylglycerol acyltransferase
wax ester synthases/acyl-CoA:diacylglycerol acyltransferases
-
wax synthase
waxester/diacylglycerol acyltransferase
WE synthase
WS/DGAT
WS2
WSD1
WSD4
WSD5
additional information
unspecific bifunctional wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase
-
-
unspecific bifunctional wax ester synthase/acyl coenzyme A:diacylglycerol acyltransferase
-
-
wax ester synthase/acyl-CoA:diacylglycerol acyltransferase
-
wax ester synthase/diacylglycerol acyltransferase
bifunctional enzyme
wax ester synthase/diacylglycerol acyltransferase
bifunctional enzyme
wax synthase
-
additional information
-
cf. EC 2.3.1.20, the enzyme belongs to the WS/DGAT family
additional information
-
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
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + a long-chain alcohol = CoA + a long-chain ester
reaction mechanism
-
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
-
-
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
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PATHWAY SOURCE
PATHWAYS
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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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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
-
?
1-decanol + palmitoyl-CoA
decyl palmitate + CoA
48% the rate of hexacedanol
-
?
1-hexadecanethiol + palmitoyl-CoA
palmitic acid hexadecane thio ester
10.4% the rate of hexanol
-
?
1-S-monopalmitoyloctanedithiol + palmitoyl-CoA
1,8-dipalmitoyloctanedithiol + CoA
13.4% the rate of hexanol
-
?
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
-
?
2-decanol + palmitoyl-CoA
dec-2-yl palmitate + CoA
38.8% the rate of hexacedanol
-
?
4-decanol + palmitoyl-CoA
4-decyl palmitate + CoA
15.6% the rate of hexacedanol
-
?
acyl-CoA + decanol
CoA + acyl decanoate
-
-
?
acyl-CoA + dodecanol
CoA + acyl dodecanoate
-
-
?
acyl-CoA + hexadecanol
CoA + acyl hexadecanoate
-
-
?
acyl-CoA + octadecanol
CoA + acyl octadecanoate
-
-
?
arachidonoyl-CoA + hexadecanol
CoA + arachidonoyl hexadecanate
-
-
?
cyclododecanol + palmitoyl-CoA
cyclododecyl palmitate + CoA
79.7% the rate of hexacedanol
-
?
cyclohexandiol + palmitoyl-CoA
? + CoA
4.1% the rate of hexacedanol
-
?
cyclohexanol + palmitoyl-CoA
cyclohexyl palmitate + CoA
32% the rate of hexacedanol
-
?
cyclohexanone oxime + palmitoyl-CoA
? + CoA
5.2% the rate of hexacedanol
-
?
decanol + palmitoyl-CoA
decanyl palmitate + CoA
-
and undecanol, best substrates
-
?
decanoyl-CoA + hexadecanol
CoA + decanoyl hexadecanate
-
-
?
decanoyl-CoA + linolenyl alcohol
?
low activity
-
?
decanoyl-CoA + linoleyl alcohol
?
low activity
-
?
decanoyl-CoA + ricinoleyl alcohol
?
low activity
-
?
eicosanoyl-CoA + cis-11-eicosenol
cis-11-eicosenyl eicosanoate + CoA
-
cis-11-eicosenol is the best acceptor
-
?
eicosanoyl-CoA + cis-13-eicosenol
cis-13-eicosenyl eicosanoate + CoA
-
-
-
?
eicosanoyl-CoA + cis-9-octadecenol
cis-9-octadecenyl eicosanoate + CoA
-
-
-
?
eicosanoyl-CoA + docosanol
docosanyl eicosanoate + CoA
-
low activity
-
?
eicosanoyl-CoA + eicosanol
eicosanyl eicosanoate + CoA
-
low activity
-
?
eicosanoyl-CoA + octadecanol
octadecanyl eicosanoate + CoA
-
low activity
-
?
eicosapentaenoyl-CoA + hexadecan-1-ol
?
-
-
?
eicosapentaenoyl-CoA + hexadecanol
CoA + eicosapentaoenoyl hexadecanate
-
-
?
eicosenoyl-CoA + docosenol
docosenoyl eicosenate + CoA
-
high activity
-
?
eicosenoyl-CoA + dodecanol
dodecanoyl eicosenate + CoA
-
high activity
-
?
eicosenoyl-CoA + hexadecanol
hexadecanoyl eicosenate + CoA
-
high activity
-
?
eicosenoyl-CoA + octadecenol
octadecenyl eicosenoate + CoA
best substrates
-
?
eicosenoyl-CoA + tetradecanol
tetradecanoyl eicosenate + CoA
-
high activity
-
?
hexadecanol + palmitoyl-CoA
hexadecyl palmitate + CoA
-
-
?
lauroyl-CoA + ricinoleyl alcohol
?
high activity
-
?
lauryol-CoA + hexadecanol
hexadecanoyl laurate + CoA
-
high activity
-
?
linoleoyl-CoA + dodecanol
dodecanoyl linoleate + CoA
-
high activity
-
?
linoleoyl-CoA + hexadecanol
hexadecanoyl linoleate + CoA
-
high activity
-
?
myristoyl-CoA + (9Z)-hexadec-9-en-1-ol
(9Z)-hexadec-9-en-1-yl tetradecanoate + CoA
-
-
?
myristoyl-CoA + 11-cis-retinol
11-cis-retinyl myristate + CoA
preferred substrate
-
?
myristoyl-CoA + all-trans-retinol
all-trans-retinyl myristate + CoA
-
-
?
myristoyl-CoA + eicosenol
eicosenoyl myristate + CoA
-
highest activity
-
?
myristoyl-CoA + hexadecanol
hexadecanoyl myristate + CoA
-
high activity
-
?
myristoyl-CoA + hexadecenol
hexadecenoyl myristate + CoA
-
high activity
-
?
myristoyl-CoA + linolenyl alcohol
?
high activity
-
?
myristoyl-CoA + linolenyl alcohol
linolenoyl myristate + CoA
-
high activity
-
?
myristoyl-CoA + linoleyl alcohol
?
high activity
-
?
myristoyl-CoA + linoleyl alcohol
linoleoyl myristate + CoA
-
high activity
-
?
myristoyl-CoA + octadecanol
octadecanoyl myristate + CoA
-
high activity
-
?
myristoyl-CoA + octadecenol
octadecenoyl myristate + CoA
-
high activity
-
?
myristoyl-CoA + tetracosanol
?
very low activity
-
?
myristoyl-CoA + tetradecanol
?
highest activity
-
?
myristoyl-CoA + tetradecanol
myristoyl myristate + CoA
100% conversion efficiency
-
?
octadecatrienoyl-CoA + hexadecan-1-ol
?
-
-
?
octadecatrienoyl-CoA + hexadecanol
CoA + octadecatrienoyl hexadecanate
-
-
?
octanoyl-CoA + hexadecanol
CoA + octanoyl hexadecanate
-
-
?
oleoyl-CoA + (9Z)-hexadec-9-en-1-ol
CoA + (9Z)-hexadec-9-en-1-yl (9Z)-octadec-9-enoate
-
-
?
oleoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 1,2-dipalmitoyl-3-oleoyl-sn-glycerol
-
-
-
?
oleoyl-CoA + eicosanol
CoA + icosyl (9Z)-octadec-9-enoate
-
-
?
oleoyl-CoA + linolenyl alcohol
?
high activity
-
?
oleoyl-CoA + linoleyl alcohol
?
high activity
-
?
oleoyl-CoA + oleic alcohol
CoA + (9Z)-octadec-9-en-1-yl (9Z)-octadec-9-enoate
-
-
?
oleoyl-CoA + tetradecanol
tetradecanoyl oleate + CoA
-
high activity
-
?
palmitoleoyl-CoA + cetyl alcohol
CoA + cetyl palmitoleate
-
-
?
palmitoleoyl-CoA + tetradecanol
tetradecyl (9Z)-hexadec-9-enoate + CoA
enzyme shows preference towards myristic acid and palmitoleyl-CoA
-
?
palmitoleyl alcohol + oleoyl-CoA
CoA + palmitoleyl oleate
-
-
?
palmitoyl-CoA + 1-hexadecanol
palmitic acid hexadecyl ester + CoA
-
highest activity
-
?
palmitoyl-CoA + butanol
butyl palmitate + CoA
50% of the rate with decanol
-
?
palmitoyl-CoA + cetyl alcohol
CoA + cetyl palmitate
-
-
?
palmitoyl-CoA + decanol
decyl palmitate + CoA
best substrate
-
?
palmitoyl-CoA + eicosenol
eicosenoyl palmitate + CoA
-
high activity
-
?
palmitoyl-CoA + ethanol
ethyl palmitate + CoA
24% of the rate with decanol
-
?
palmitoyl-CoA + hexadecan-1-ol
CoA + hexadecyl palmitate
-
-
?
palmitoyl-CoA + hexadecanol
CoA + palmitoyl hexadecanate
-
-
?
palmitoyl-CoA + hexadecanol
hexadecanoyl palmitate + CoA
-
high activity
-
?
palmitoyl-CoA + hexadecanol
hexadecyl palmitate + CoA
79% of the rate with decanol
-
?
palmitoyl-CoA + hexadecanol
palmitoyl palmitate + CoA
about 25% conversion efficiency compared to myristoyl-CoA plus tetradecanol
-
?
palmitoyl-CoA + hexanol
hexyl palmitate + CoA
87% of the rate with decanol
-
?
palmitoyl-CoA + isoamyl alcohol
isoamyl palmitate + CoA
57% of the rate with decanol
-
?
palmitoyl-CoA + long-chain fatty alcohol
CoA + long-chain palmitoyl ester
-
-
-
?
palmitoyl-CoA + octadecenol
octadecenoyl palmitate + CoA
-
high activity
-
?
palmitoyl-CoA + octanol
octyl palmitate + CoA
79% of the rate with decanol
-
?
palmitoyl-CoA + ricinoleyl alcohol
?
high activity
-
?
palmitoyl-CoA + tetracosanol
?
very low activity
-
?
palmitoyl-CoA + tetradecanol
tetradecanoyl palmitate + CoA
-
high activity
-
?
phenol + palmitoyl-CoA
phenyl palmitate + CoA
4.1% the rate of hexacedanol
-
?
phenylethanol + palmitoyl-CoA
phenylethyl palmitate + CoA
99% the rate of hexacedanol
-
?
stearoyl-CoA + hexadecanol
CoA + stearoyl hexadecanate
-
-
?
stearoyl-CoA + tetradecanol
tetradecanoyl stearate + CoA
-
high activity
-
?
1-hexadecanethiol + palmitoyl-CoA
palmitic acid hexadecyl thio ester + CoA
-
-
-
?
1-hexadecanethiol + palmitoyl-CoA
palmitic acid hexadecyl thio ester + CoA
-
mutant strain ADP1acr1omegaKm
-
?
1-hexadecanol + palmitoyl-CoA
palmitic acid hexadecyl ester + CoA
-
best substrate
-
?
1-hexadecanol + palmitoyl-CoA
palmitic acid hexadecyl ester + CoA
-
mutant strain ADP1acr1omegaKm
-
?
1-S-monopalmitoyloctanedithiol + palmitoyl-CoA
1,8-S-dipalmitoyloctanedithiol + CoA
-
-
-
?
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
-
-
1-S-monopalmitoyloctanedithiol is the main product
?
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
?
2 1,8-octanedithiol + 3 palmitoyl-CoA
1-S-monopalmitoyloctanedithiol + 1,8-S-dipalmitoyloctanedithiol + 3 CoA
-
-
1-S-monopalmitoyloctanedithiol is the main product
?
2-phenylethanol + palmitoyl-CoA
2-phenylethyl palmitate + CoA
-
-
?
2-phenylethanol + palmitoyl-CoA
2-phenylethyl palmitate + CoA
-
-
?
acyl-CoA + a long-chain alcohol
CoA + a long-chain ester
-
-
?
acyl-CoA + a long-chain alcohol
CoA + a long-chain ester
-
-
-
?
acyl-CoA + a long-chain alcohol
CoA + a long-chain ester
-
-
-
?
acyl-CoA + a long-chain alcohol
CoA + a long-chain ester
-
-
?
acyl-CoA + long-chain diacylglycerol
CoA + long-chain triacylglycerol
-
-
-
?
acyl-CoA + long-chain diacylglycerol
CoA + long-chain triacylglycerol
-
-
?
acyl-CoA + long-chain fatty alcohol
CoA + long-chain fatty ester
-
-
-
?
acyl-CoA + long-chain fatty alcohol
CoA + long-chain fatty ester
-
-
?
acyl-CoA + long-chain fatty alcohol
CoA + long-chain fatty ester
-
-
-
?
dodecan-1-ol + palmitoyl-CoA
CoA + dodecanyl palmitate
-
-
?
dodecan-1-ol + palmitoyl-CoA
CoA + dodecanyl palmitate
-
-
?
dodecanol + palmitoyl-CoA
dodecanyl palmitate + CoA
-
best substrate
-
?
dodecanol + palmitoyl-CoA
dodecanyl palmitate + CoA
-
and undecanol, best substrates for both isoforms Ma1 and Ma2
-
?
dodecanol + palmitoyl-CoA
dodecanyl palmitate + CoA
-
-
-
?
ethanol + palmitoyl-CoA
ethyl palmitate + CoA
-
-
?
ethanol + palmitoyl-CoA
ethyl palmitate + CoA
-
-
?
hexadecan-1-ol + palmitoyl-CoA
CoA + hexadecyl palmitate
-
-
?
hexadecan-1-ol + palmitoyl-CoA
CoA + hexadecyl palmitate
-
-
?
hexadecanol + palmitoyl-CoA
hexadecanyl palmitate + CoA
-
-
-
?
hexadecanol + palmitoyl-CoA
hexadecanyl palmitate + CoA
-
-
-
?
hexadecanol + palmitoyl-CoA
hexadecanyl palmitate + CoA
-
-
-
?
hexan-1-ol + palmitoyl-CoA
hexyl palmitate + CoA
-
-
?
hexan-1-ol + palmitoyl-CoA
hexyl palmitate + CoA
-
-
?
isoamyl alcohol + palmitoyl-CoA
isoamyl palmitate + CoA
-
-
?
isoamyl alcohol + palmitoyl-CoA
isoamyl palmitate + CoA
-
-
?
lauroyl-CoA + hexadecanol
CoA + lauroyl hexadecanate
-
-
?
lauroyl-CoA + hexadecanol
CoA + lauroyl hexadecanate
best acyl-CoA substrate
-
?
linoleoyl-CoA + tetradecanol
tetradecanoyl linoleate + CoA
-
high activity
-
?
linoleoyl-CoA + tetradecanol
tetradecanoyl linoleate + CoA
-
second highest activity
-
?
myristoyl-CoA + hexadecanol
CoA + myristoyl hexadecanate
-
-
?
myristoyl-CoA + hexadecanol
CoA + myristoyl hexadecanate
preferred acyl-CoA substrate
-
?
nonan-1-ol + palmitoyl-CoA
CoA + nonyl palmitate
-
-
?
nonan-1-ol + palmitoyl-CoA
CoA + nonyl palmitate
-
-
?
palmitoyl-CoA + hexadecanol
CoA + hexadecyl palmitate
-
-
-
?
palmitoyl-CoA + octadecanol
octadecanoyl palmitate + CoA
-
high activity
-
?
palmitoyl-CoA + octadecanol
octadecanoyl palmitate + CoA
-
lowest activity
-
?
tetradecanol + palmitoyl-CoA
tetradecanyl palmitate + CoA
-
best substrate
-
?
tetradecanol + palmitoyl-CoA
tetradecanyl palmitate + CoA
-
best substrate
-
?
undecanol + palmitoyl-CoA
undecanyl palmitate + CoA
-
and dodecanol, best substrates for both isoforms Ma1 and Ma2
-
?
undecanol + palmitoyl-CoA
undecanyl palmitate + CoA
-
and decanol, best substrates
-
?
undecanol + palmitoyl-CoA
undecanyl palmitate + CoASH
-
-
-
?
additional information
?
-
-
key enzyme in the biosynthesis of neutral lipid storage compounds, triacylglycerols and wax esters, overview
-
?
additional information
?
-
-
a bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
-
?
additional information
?
-
-
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
-
?
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 enzyme has high preference for C18 substrates
-
-
additional information
?
-
Acinetobacter baylyi ATCC 3305
the enzyme has high preference for C18 substrates
-
-
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 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
-
?
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 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
-
?
additional information
?
-
-
the enzyme plays the key role in the biosynthesis of triacylglycerols and wax esters, overview
-
?
additional information
?
-
-
acyl acceptor specificities of isozymes AtfA1 and AtfA2 from A. borkumensis SK2 for glycerol and acylglycerols, 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 has a high level of wax synthase activity and approximately 10fold lower level of diacylglycerol acyltransferase activity
-
?
additional information
?
-
isoform WSD2 has a high specificity toward shorter chain length fatty acids and alcohols and readily utilize C14 fatty acid and C14 alcohol as substrates, show low activity with C16 substrates, and almost negligible reaction toward C18 substrates
-
-
additional information
?
-
isoform WSD2 has a high specificity toward shorter chain length fatty acids and alcohols and readily utilize C14 fatty acid and C14 alcohol as substrates, show low activity with C16 substrates, and almost negligible reaction toward C18 substrates
-
-
additional information
?
-
-
isoform WSD2 has a high specificity toward shorter chain length fatty acids and alcohols and readily utilize C14 fatty acid and C14 alcohol as substrates, show low activity with C16 substrates, and almost negligible reaction toward C18 substrates
-
-
additional information
?
-
isoform WSD5 has a high specificity toward shorter chain length fatty acids and alcohols and readily utilize C14 fatty acid and C14 alcohol as substrates, show low activity with C16 substrates, and almost negligible reaction toward C18 substrates
-
-
additional information
?
-
isoform WSD5 has a high specificity toward shorter chain length fatty acids and alcohols and readily utilize C14 fatty acid and C14 alcohol as substrates, show low activity with C16 substrates, and almost negligible reaction toward C18 substrates
-
-
additional information
?
-
-
isoform WSD5 has a high specificity toward shorter chain length fatty acids and alcohols and readily utilize C14 fatty acid and C14 alcohol as substrates, show low activity with C16 substrates, and almost negligible reaction toward C18 substrates
-
-
additional information
?
-
no activity with stearoyl-CoA and octadecanol as substrates
-
-
additional information
?
-
no activity with stearoyl-CoA and octadecanol as substrates
-
-
additional information
?
-
-
no activity with stearoyl-CoA and octadecanol as substrates
-
-
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
?
-
-
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
-
?
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 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
-
?
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
-
?
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
?
-
bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
-
?
additional information
?
-
bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
-
?
additional information
?
-
bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20
-
?
additional information
?
-
-
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 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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
-
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
-
?
additional information
?
-
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
-
?
additional information
?
-
-
the enzyme is involved in synthesis of isoprenoid wax ester storage compounds, pathway, overview
-
?
additional information
?
-
-
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
-
?
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 enzyme has high preference for C18 substrates
-
-
additional information
?
-
the enzyme shows no diacylglycerol acyltransferase activity
-
-
additional information
?
-
-
the enzyme shows no diacylglycerol acyltransferase activity
-
-
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 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
-
?
additional information
?
-
-
the purified enzyme AtfG25 shows acyltransferase activity with C12- or C16-acyl-CoA (cf. EC 2.3.1.20), C2 to C18 alcohols (ethanol, butanol, hexanol, octanol, decanol, dodecanol, tetradecanol, hexadecanol, palmitoleyl alcohol, and octadecanol), and dipalmitoyl glycerol. Substrate specificity, overview. The DGAT activity of AtfG25 corresponds to about 70% of itsWS activity
-
-
additional information
?
-
the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity, overview. TrWSD4 accepts four linear alcohols as substrates and the highest WS activity is observed for octadecanol (C18:0-OH), which is 2fold higher than the activity using decanol as substrate (C10:0-OH)
-
-
additional information
?
-
the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity, overview. TrWSD4 accepts four linear alcohols as substrates and the highest WS activity is observed for octadecanol (C18:0-OH), which is 2fold higher than the activity using decanol as substrate (C10:0-OH)
-
-
additional information
?
-
-
the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity, overview. TrWSD4 accepts four linear alcohols as substrates and the highest WS activity is observed for octadecanol (C18:0-OH), which is 2fold higher than the activity using decanol as substrate (C10:0-OH)
-
-
additional information
?
-
the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity, overview. TrWSD5 accepts four linear alcohols as substrates and the highest WS activity is observed for octadecanol (C18:0-OH), which is 2fold higher than the activity using decanol as substrate (C10:0-OH)
-
-
additional information
?
-
the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity, overview. TrWSD5 accepts four linear alcohols as substrates and the highest WS activity is observed for octadecanol (C18:0-OH), which is 2fold higher than the activity using decanol as substrate (C10:0-OH)
-
-
additional information
?
-
-
the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity, overview. TrWSD5 accepts four linear alcohols as substrates and the highest WS activity is observed for octadecanol (C18:0-OH), which is 2fold higher than the activity using decanol as substrate (C10:0-OH)
-
-
additional information
?
-
Thraustochytrium roseum ATCC28210
the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity, overview. TrWSD4 accepts four linear alcohols as substrates and the highest WS activity is observed for octadecanol (C18:0-OH), which is 2fold higher than the activity using decanol as substrate (C10:0-OH)
-
-
additional information
?
-
Thraustochytrium roseum ATCC28210
the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity, overview. TrWSD4 accepts four linear alcohols as substrates and the highest WS activity is observed for octadecanol (C18:0-OH), which is 2fold higher than the activity using decanol as substrate (C10:0-OH)
-
-
additional information
?
-
Thraustochytrium roseum ATCC28210
the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity, overview. TrWSD5 accepts four linear alcohols as substrates and the highest WS activity is observed for octadecanol (C18:0-OH), which is 2fold higher than the activity using decanol as substrate (C10:0-OH)
-
-
additional information
?
-
Thraustochytrium roseum ATCC28210
the recombinant protein purified from Escherichia coli strain Rosetta (DE3) has substantial wax synthase (WS) and lower diacylglycerol acyltransferase (DGAT) activity. Acyl-CoA substrate specificity, overview. TrWSD5 accepts four linear alcohols as substrates and the highest WS activity is observed for octadecanol (C18:0-OH), which is 2fold higher than the activity using decanol as substrate (C10:0-OH)
-
-
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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
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
-
-
-
?
acyl-CoA + a long-chain alcohol
CoA + a long-chain ester
-
-
-
?
acyl-CoA + a long-chain alcohol
CoA + a long-chain ester
-
-
-
-
?
acyl-CoA + a long-chain alcohol
CoA + a long-chain ester
-
-
-
-
?
acyl-CoA + a long-chain alcohol
CoA + a long-chain ester
-
-
-
?
acyl-CoA + long-chain fatty alcohol
CoA + long-chain fatty ester
-
-
-
?
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 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
?
-
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
?
-
-
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11-cis-retinyl acetate
the presence of 11-cis-retinyl acetate leads to reduction in esterification of 9-cis-retinol
-
11-cis-retinyl laurate
the presence of 11-cis-retinyl laurate leads to reduction in esterification of 9-cis-retinol
-
11-cis-retinyl palmitate
the presence of 0.01 mM 11-cis-retinyl palmitate significantly reduces the amount of 9-cis-retinyl ester produced by the enzyme. 11-cis-retinyl palmitate also inhibits13-cis- and all-trans-retinol esterification, but has no effect on formation of 11-cis-retinyl myristate
oleoyl-CoA
substrate inhibition; substrate inhibition
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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
-
bovine serum albumin
-
highest activity in the presence of 0.6 mg bovine serum albumin
-
NaCl
isoform WSD4 shows maximum enzyme activity at NaCl concentration of 400 mM
NaCl
isoform WSD5 shows maximum enzyme activity at NaCl concentration of 800 mM
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Ectodermal Dysplasia
A novel large deletion that encompasses EDA and the downstream gene AWAT2 causes X-linked hypohidrotic/anhidrotic ectodermal dysplasia.
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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
0.22635
Arachidonoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.2264
Arachidonoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.29717
Arachidonoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.2972
Arachidonoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.00096
decanoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.001
decanoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.0176
decanoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.0176
decanoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.10162
eicosapentaenoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.1062
eicosapentaenoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.13116
eicosapentaenoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.1312
eicosapentaenoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.00014
lauroyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.00014
lauroyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.0259
lauroyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.02593
lauroyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.00394
myristoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.00394
myristoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.0185
myristoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.0185
myristoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.28086
octadecatrienoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
-
0.2809
octadecatrienoyl-CoA
pH 7.4, 37°C, recombinant enzyme
-
0.28468
octadecatrienoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
-
0.2847
octadecatrienoyl-CoA
pH 7.4, 37°C, recombinant enzyme
-
0.01225
octanoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.0123
octanoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.02993
octanoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.02993
octanoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.00308
palmitoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.00308
palmitoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.02477
palmitoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.0248
palmitoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.01915
stearoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.01915
stearoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.07587
stearoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.0759
stearoyl-CoA
pH 7.4, 37°C, recombinant enzyme
additional information
additional information
-
kinetics of isozymes WS1 and WS2
-
additional information
additional information
kinetics of wax synthase activity, overview
-
additional information
additional information
kinetics of wax synthase activity, overview
-
additional information
additional information
-
kinetics of wax synthase activity, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0148
Arachidonoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.0148
Arachidonoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.165
Arachidonoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.165
Arachidonoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.00941
decanoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.0154
decanoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.0154
decanoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.0941
decanoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.0114
eicosapentaenoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.0114
eicosapentaenoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.498
eicosapentaenoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.498
eicosapentaenoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.0202
lauroyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.0202
lauroyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.243
lauroyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.243
lauroyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.0254
myristoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.0254
myristoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.331
myristoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.331
myristoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.0236
octadecatrienoyl-CoA
pH 7.4, 37°C, recombinant enzyme
-
0.0236
octadecatrienoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
-
0.242
octadecatrienoyl-CoA
pH 7.4, 37°C, recombinant enzyme
-
0.242
octadecatrienoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
-
0.0185
octanoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.0185
octanoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.102
octanoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.102
octanoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.032
palmitoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.032
palmitoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.341
palmitoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.341
palmitoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.0379
stearoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.0379
stearoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.604
stearoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.604
stearoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0488
Arachidonoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.05
Arachidonoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.729
Arachidonoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.73
Arachidonoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.873
decanoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.875
decanoyl-CoA
pH 7.4, 37°C, recombinant enzyme
98.02
decanoyl-CoA
pH 7.4, 37°C, recombinant enzyme
98.3
decanoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.0866
eicosapentaenoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
0.087
eicosapentaenoyl-CoA
pH 7.4, 37°C, recombinant enzyme
4.69
eicosapentaenoyl-CoA
pH 7.4, 37°C, recombinant enzyme
4.69
eicosapentaenoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
9.37
lauroyl-CoA
pH 7.4, 37°C, recombinant enzyme
9.37
lauroyl-CoA
isoform WSD5, at pH 7.4 and 37°C
144.29
lauroyl-CoA
pH 7.4, 37°C, recombinant enzyme
146
lauroyl-CoA
isoform WSD4, at pH 7.4 and 37°C
6.44
myristoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
6.45
myristoyl-CoA
pH 7.4, 37°C, recombinant enzyme
17.89
myristoyl-CoA
pH 7.4, 37°C, recombinant enzyme
17.9
myristoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
0.084
octadecatrienoyl-CoA
pH 7.4, 37°C, recombinant enzyme
-
0.084
octadecatrienoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
-
0.85
octadecatrienoyl-CoA
pH 7.4, 37°C, recombinant enzyme
-
0.85
octadecatrienoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
-
0.618
octanoyl-CoA
pH 7.4, 37°C, recombinant enzyme
0.619
octanoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
8.33
octanoyl-CoA
pH 7.4, 37°C, recombinant enzyme
8.33
octanoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
10.39
palmitoyl-CoA
pH 7.4, 37°C, recombinant enzyme
10.4
palmitoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
13.7
palmitoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
13.77
palmitoyl-CoA
pH 7.4, 37°C, recombinant enzyme
1.98
stearoyl-CoA
pH 7.4, 37°C, recombinant enzyme
1.98
stearoyl-CoA
isoform WSD4, at pH 7.4 and 37°C
7.96
stearoyl-CoA
pH 7.4, 37°C, recombinant enzyme
7.96
stearoyl-CoA
isoform WSD5, at pH 7.4 and 37°C
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Ki VALUE [mM]
INHIBITOR
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
140
substrate nonan-1-ol, wild-type, 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
1700
substrate dodecan-1-ol, mutant G355I, 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
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
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
360
substrate nonan-1-ol, mutant G355I, 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
7.8
substrate nonan-1-ol, mutant A360F, pH not specified in the publication, temperature not specified in the publication
70
substrate hexadecan-1-ol, wild-type, pH not specified in the publication, temperature not specified in the publication
80
substrate hexadecan-1-ol, mutant G355I, pH not specified in the publication, temperature not specified in the publication
960
substrate dodecan-1-ol, wild-type, 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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
the activity of the enzyme gradually increases with the raise of buffer pH reaching the maximum at pH around 7.0
7.4
additional information
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
more than 50% activity between pH 6.0 and 8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17 - 47
the enzyme activity of isoform WSD5 is stable when the temperature increases from 17 to 47°C
7 - 57
7 - 57
activity range, the WS activity of TrWSD4 is gradually increased when the temperature is increased from 7 to 47°C, while it decreases to 92% of the highest enzyme activity when the temperature reaches 57°C. Influence of increasing temperature on saturation curves using palmitoyl-CoA and hexadecanol as substrates, overview
7 - 57
enzyme activity of Isoform WSD4 is gradually increased when the temperature is increased from 7 to 47°C while decrease to 92% of the highest enzyme activity when the temperature reaches 57°C
7 - 57
the lowest WS activity of TrWSD5 is observed at the lowest and the highest temperatures tested in this assay. The enzyme activity of TrWSD5 appears to be stable when the temperature increases from 17 to 47°C. Influence of increasing temperature on saturation curves using palmitoyl-CoA and hexadecanol as substrates, overview
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.05
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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
-
-
brenda