Information on EC 2.3.1.75 - long-chain-alcohol O-fatty-acyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
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 hide
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + a long-chain alcohol = CoA + a long-chain ester
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cuticular wax biosynthesis
-
-
long chain fatty acid ester synthesis (engineered)
-
-
wax esters biosynthesis I
-
-
wax esters biosynthesis II
-
-
Cutin, suberine and wax biosynthesis
-
-
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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 hide
64060-40-8
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
formerly Acinetobacter calcoaceticus ADP1
-
-
Manually annotated by BRENDA team
a marine hydrocarbonoclastic bacterium, strain SK2 and several mutant strains, overview, genes atfA1, ABO_2742 and atfA2, ABO_1804, encoding isozymes AtfA1 and AtfA2
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
isozymes AWAT1 and AWAT2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-hexadecandiol + palmitoyl-CoA
?
show the reaction diagram
1,8-octanedithiol + palmitoyl-CoA
1-S-monopalmitoyloctanedithiol + CoA
show the reaction diagram
59.3% the rate of hexadecanol, plus minor amounts of 1,8-dipalmitoyloctanedithiol
-
-
?
1-decanol + palmitoyl-CoA
decyl palmitate + CoA
show the reaction diagram
48% the rate of hexacedanol
-
-
?
1-hexadecanethiol + palmitoyl-CoA
palmitic acid hexadecane thio ester
show the reaction diagram
10.4% the rate of hexanol
-
-
?
1-hexadecanethiol + palmitoyl-CoA
palmitic acid hexadecyl thio ester + CoA
show the reaction diagram
1-hexadecanol + palmitoyl-CoA
CoA + hexadecylpalmitate
show the reaction diagram
1-hexadecanol + palmitoyl-CoA
palmitic acid hexadecyl ester + CoA
show the reaction diagram
1-hexanol + palmitoyl-CoA
hexyl palmitate + CoA
show the reaction diagram
-
-
-
?
1-S-monopalmitoyloctanedithiol + palmitoyl-CoA
1,8-dipalmitoyloctanedithiol + CoA
show the reaction diagram
13.4% the rate of hexanol
-
-
?
1-S-monopalmitoyloctanedithiol + palmitoyl-CoA
1,8-S-dipalmitoyloctanedithiol + CoA
show the reaction diagram
2 1,8-octanedithiol + 3 palmitoyl-CoA
1-S-monopalmitoyloctanedithiol + 1,8-S-dipalmitoyloctanedithiol + 3 CoA
show the reaction diagram
2-cyclohexylethanol + palmitoyl-CoA
2-cyclohexylethyl palmitate + CoA
show the reaction diagram
44.8% the rate of hexacedanol
-
-
?
2-decanol + palmitoyl-CoA
dec-2-yl palmitate + CoA
show the reaction diagram
38.8% the rate of hexacedanol
-
-
?
2-phenylethanol + palmitoyl-CoA
2-phenylethyl palmitate + CoA
show the reaction diagram
4-decanol + palmitoyl-CoA
4-decyl palmitate + CoA
show the reaction diagram
15.6% the rate of hexacedanol
-
-
?
acyl-CoA + long-chain diacylglycerol
CoA + long-chain triacylglycerol
show the reaction diagram
acyl-CoA + long-chain fatty alcohol
CoA + long-chain fatty ester
show the reaction diagram
cetyl alcohol + oleoyl-CoA
CoA + cetyloleate
show the reaction diagram
-
-
-
?
cis-11-eicosenol + acetyl-CoA
cis-11-eicosenyl acetate + CoA
show the reaction diagram
-
-
-
-
?
cyclododecanol + palmitoyl-CoA
cyclododecyl palmitate + CoA
show the reaction diagram
79.7% the rate of hexacedanol
-
-
?
cyclohexandiol + palmitoyl-CoA
? + CoA
show the reaction diagram
4.1% the rate of hexacedanol
-
-
?
cyclohexanol + palmitoyl-CoA
cyclohexyl palmitate + CoA
show the reaction diagram
32% the rate of hexacedanol
-
-
?
cyclohexanone oxime + palmitoyl-CoA
? + CoA
show the reaction diagram
5.2% the rate of hexacedanol
-
-
?
decanol + palmitoyl-CoA
decanyl palmitate + CoA
show the reaction diagram
-
and undecanol, best substrates
-
-
?
dodecan-1-ol + palmitoyl-CoA
CoA + dodecanyl palmitate
show the reaction diagram
dodecanol + palmitoyl-CoA
dodecanyl palmitate + CoA
show the reaction diagram
eicosanoyl-CoA + cis-11-eicosenol
cis-11-eicosenyl eicosanoate + CoA
show the reaction diagram
-
cis-11-eicosenol is the best acceptor
-
-
?
eicosanoyl-CoA + cis-13-eicosenol
cis-13-eicosenyl eicosanoate + CoA
show the reaction diagram
-
-
-
-
?
eicosanoyl-CoA + cis-9-octadecenol
cis-9-octadecenyl eicosanoate + CoA
show the reaction diagram
-
-
-
-
?
eicosanoyl-CoA + decanol
decanyl eicosanoate + CoA
show the reaction diagram
-
low activity
-
-
?
eicosanoyl-CoA + docosanol
docosanyl eicosanoate + CoA
show the reaction diagram
-
low activity
-
-
?
eicosanoyl-CoA + dodecanol
dodecanyl eicosanoate + CoA
show the reaction diagram
-
-
-
-
?
eicosanoyl-CoA + eicosanol
eicosanyl eicosanoate + CoA
show the reaction diagram
-
low activity
-
-
?
eicosanoyl-CoA + hexadecanol
hexadecanyl eicosanoate + CoA
show the reaction diagram
-
-
-
-
?
eicosanoyl-CoA + octadecanol
octadecanyl eicosanoate + CoA
show the reaction diagram
-
low activity
-
-
?
eicosanoyl-CoA + tetradecanol
tetradecanyl eicosanoate + CoA
show the reaction diagram
-
-
-
-
?
eicosenoyl-CoA + docosenol
docosenyl eicosenoate + CoA
show the reaction diagram
-
-
-
ir
eicosenoyl-CoA + octadecenol
octadecenyl eicosenoate + CoA
show the reaction diagram
best substrates
-
-
?
ethanol + palmitoyl-CoA
ethyl palmitate + CoA
show the reaction diagram
hexadecan-1-ol + palmitoyl-CoA
CoA + hexadecyl palmitate
show the reaction diagram
hexadecanol + palmitoyl-CoA
hexadecanyl palmitate + CoA
show the reaction diagram
hexadecanol + palmitoyl-CoA
hexadecyl palmitate + CoA
show the reaction diagram
-
-
-
?
hexan-1-ol + palmitoyl-CoA
hexyl palmitate + CoA
show the reaction diagram
isoamyl alcohol + palmitoyl-CoA
isoamyl palmitate + CoA
show the reaction diagram
lauryl-CoA + myristic acid
lauryl myristate
show the reaction diagram
-
-
-
?
lauryl-CoA + tetradecanol
tetradecanyl laurate + CoA
show the reaction diagram
-
-
-
-
?
linear long-chain alcohol + oleoyl-CoA
?
show the reaction diagram
-
-
-
?
linear long-chain alcohol + palmitoleoyl-CoA
?
show the reaction diagram
-
-
-
?
linear long-chain alcohol + palmitoyl-CoA
?
show the reaction diagram
-
-
-
?
linear long-chain alcohol + stearoyl-CoA
?
show the reaction diagram
-
-
-
?
myristoyl-CoA + dodecan-1-ol
dodecan-1-yl myristate + CoA
show the reaction diagram
myristyl-CoA + myristic acid
myristyl myristate
show the reaction diagram
-
-
-
?
myristyl-CoA + palmitic acid
myristyl palmitate
show the reaction diagram
-
-
-
?
myristyl-CoA + palmitoleic acid
myristyl palmitoleate
show the reaction diagram
-
-
-
?
nonan-1-ol + palmitoyl-CoA
CoA + nonyl palmitate
show the reaction diagram
octadecenoyl-CoA + dodecanol
dodecanyl octadecanoate + CoA
show the reaction diagram
-
-
-
-
ir
oleoyl-CoA + (9Z)-hexadec-9-en-1-ol
CoA + (9Z)-hexadec-9-en-1-yl (9Z)-octadec-9-enoate
show the reaction diagram
-
-
-
-
oleoyl-CoA + 1,2-dipalmitoyl-sn-glycerol
CoA + 1,2-dipalmitoyl-3-oleoyl-sn-glycerol
show the reaction diagram
-
-
-
-
-
oleoyl-CoA + 1-decanol
CoA + decyl oleate
show the reaction diagram
-
-
-
-
oleoyl-CoA + 1-octadecanol
CoA + octadecyl oleate
show the reaction diagram
oleoyl-CoA + cetyl alcohol
CoA + cetyl oleate
show the reaction diagram
-
-
-
-
oleoyl-CoA + decanol
CoA + decyl oleate
show the reaction diagram
-
-
-
?
oleoyl-CoA + eicosanol
CoA + icosyl (9Z)-octadec-9-enoate
show the reaction diagram
oleoyl-CoA + oleic alcohol
CoA + (9Z)-octadec-9-en-1-yl (9Z)-octadec-9-enoate
show the reaction diagram
palmitoleoyl-CoA + cetyl alcohol
CoA + cetyl palmitoleate
show the reaction diagram
-
-
-
-
palmitoleyl alcohol + oleoyl-CoA
CoA + palmitoleyl oleate
show the reaction diagram
-
-
-
?
palmitoleyl-CoA + myristic acid
palmitoleyl myristate + CoA
show the reaction diagram
enzyme shows preference towards myristic acid and palmitoleyl-CoA
-
-
?
palmitoyl-CoA + 1,2-dipalmitin
?
show the reaction diagram
palmitoyl-CoA + 1,2-hexadecandiol
?
show the reaction diagram
-
-
-
-
palmitoyl-CoA + 1-hexadecanol
?
show the reaction diagram
palmitoyl-CoA + all-trans-retinol
?
show the reaction diagram
-
-
-
-
palmitoyl-CoA + butanol
butyl palmitate + CoA
show the reaction diagram
50% of the rate with decanol
-
-
?
palmitoyl-CoA + cetyl alcohol
CoA + cetyl palmitate
show the reaction diagram
-
-
-
-
palmitoyl-CoA + decanol
decyl palmitate + CoA
show the reaction diagram
best substrate
-
-
?
palmitoyl-CoA + dioleoylglycerol
?
show the reaction diagram
-
-
-
-
palmitoyl-CoA + ethanol
ethyl palmitate + CoA
show the reaction diagram
24% of the rate with decanol
-
-
?
palmitoyl-CoA + hexadecanol
CoA + hexadecyl palmitate
show the reaction diagram
palmitoyl-CoA + hexadecanol
hexadecanyl palmitate + CoA
show the reaction diagram
-
-
-
-
?
palmitoyl-CoA + hexadecanol
hexadecyl palmitate + CoA
show the reaction diagram
79% of the rate with decanol
-
-
?
palmitoyl-CoA + hexanol
hexyl palmitate + CoA
show the reaction diagram
87% of the rate with decanol
-
-
?
palmitoyl-CoA + isoamyl alcohol
isoamyl palmitate + CoA
show the reaction diagram
57% of the rate with decanol
-
-
?
palmitoyl-CoA + long-chain fatty alcohol
CoA + long-chain palmitoyl ester
show the reaction diagram
-
-
-
-
-
palmitoyl-CoA + monooleoylglycerol
?
show the reaction diagram
-
-
-
-
palmitoyl-CoA + octanol
octyl palmitate + CoA
show the reaction diagram
79% of the rate with decanol
-
-
?
palmitoyl-CoA + phytol
?
show the reaction diagram
-
-
-
-
-
palmityl-CoA + myristic acid
palmityl myristate
show the reaction diagram
-
-
-
?
phenol + palmitoyl-CoA
phenyl palmitate + CoA
show the reaction diagram
4.1% the rate of hexacedanol
-
-
?
phenylethanol + palmitoyl-CoA
phenylethyl palmitate + CoA
show the reaction diagram
99% the rate of hexacedanol
-
-
?
phytanoyl-CoA + phytol
?
show the reaction diagram
-
-
-
-
-
stearoyl-CoA + cetyl alcohol
CoA + cetyl stearate
show the reaction diagram
-
-
-
-
tetradecanol + palmitoyl-CoA
tetradecanyl palmitate + CoA
show the reaction diagram
undecanol + palmitoyl-CoA
undecanyl palmitate + CoA
show the reaction diagram
undecanol + palmitoyl-CoA
undecanyl palmitate + CoASH
show the reaction diagram
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,2-hexadecandiol + palmitoyl-CoA
?
show the reaction diagram
-
-
-
-
?
1-hexadecanethiol + palmitoyl-CoA
palmitic acid hexadecyl thio ester + CoA
show the reaction diagram
-
mutant strain ADP1acr1omegaKm
-
-
?
1-hexadecanol + palmitoyl-CoA
CoA + hexadecylpalmitate
show the reaction diagram
-
-
-
-
?
1-hexadecanol + palmitoyl-CoA
palmitic acid hexadecyl ester + CoA
show the reaction diagram
-
mutant strain ADP1acr1omegaKm
-
-
?
1-S-monopalmitoyloctanedithiol + palmitoyl-CoA
1,8-S-dipalmitoyloctanedithiol + CoA
show the reaction diagram
-
mutant strain ADP1acr1omegaKm
-
-
?
2 1,8-octanedithiol + 3 palmitoyl-CoA
1-S-monopalmitoyloctanedithiol + 1,8-S-dipalmitoyloctanedithiol + 3 CoA
show the reaction diagram
-
mutant strain ADP1acr1omegaKm
1-S-monopalmitoyloctanedithiol is the main product
-
?
acyl-CoA + long-chain diacylglycerol
CoA + long-chain triacylglycerol
show the reaction diagram
Q58HT5, Q6E213, Q6ZPD8
-
-
-
-
acyl-CoA + long-chain fatty alcohol
CoA + long-chain fatty ester
show the reaction diagram
cis-11-eicosenol + acetyl-CoA
cis-11-eicosenyl acetate + CoA
show the reaction diagram
-
-
-
-
?
additional information
?
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
activation
CTP
-
activation
UTP
-
activation
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no influence of NaCl or KCl up to 20 mM
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bovine serum albumin
-
above 5 mg/ml
-
CaCl2
5 mM, 30% inhibition
ethanol
-
substrate inhibition above 0.5 M
MgCl2
5 mM, 17% inhibition
MnCl2
5 mM, 30% inhibition
Polyvinylpyrrolidone
-
slight inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ammonium sulfate
45 mM, 10% increase in activtiy
bovine serum albumin
-
defatted, 2fold activation in crude enzyme extract at concentration below 5 mg/ml, inhibition above
-
GTP
-
activation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.044
hexadecanol
-
pH 7.4, 37°C, isozyme WS2
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
0.0156 - 0.029
palmitoyl-CoA
additional information
additional information
-
kinetics of isozymes WS1 and WS2
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4794
hexadecanol
-
pH 7.4, 37°C, isozyme WS2
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000005
-
recombinant mutant H133L
0.0000005
-
recombinant mutant H132L
0.0000414
-
recombinant mutant D137A
0.0000464
-
recombinant wild-type enzyme
0.0000517
-
recombinant mutant G138A
0.12
-
substrate hexadecanol, pH 7.0, 22°C
0.165
-
purified recombinant His-tagged enzyme
0.1652
35°C, pH 7.4
0.2128
pH 7.4, 35°C
0.24
-
substrate hexadecanol, isoform Ma2, pH 7.0, 22°C
0.275
-
purified His-tagged recombinant enzyme, with palmitoyl-CoA
0.68
-
substrate hexadecanol, isoform Ma1, pH 7.0, 22°C
0.83
-
substrate dodecanol, pH 7.0, 22°C
0.84
-
substrate dodecanol, pH 7.0, 22°C
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
3.37
-
substrate dodecanol, pH 7.0, 22°C
3.6
-
substrate nonan-1-ol, wild-type, pH not specified in the publication, temperature not specified in the publication
4.96
-
substrate dodecanol, isoform Ma2, pH 7.0, 22°C
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
37.3
-
substrate dodecanol, isoform Ma1, pH 7.0, 22°C
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at; assay at; assay at
additional information
pI: 9.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
no activity above
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.9
AWAT1, sequence calculation
9
-
AWAT1, sequence calculation
9.1
AWAT1, sequence calculation
9.4
AWAT2, sequence calculation
9.5
AWAT2, sequence calculation
9.8
-
AWAT2, sequence calculation
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cells grown on phytol as the sole carbon source under limiting nitrogen and/or phosphorous conditions
Manually annotated by BRENDA team
; very low expression level
Manually annotated by BRENDA team
very low expression level
Manually annotated by BRENDA team
; very low expression level
Manually annotated by BRENDA team
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Manually annotated by BRENDA team
additional information
-
the enzyme exhibits a very specific adsorption pattern to artificial phospholipid membranes
-
Manually annotated by BRENDA team
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
x * 30000, SDS-PAGE
37573
x * 37573, AWAT1, sequence calculation
37759
x * 37759, AWAT1, sequence calculation
38094
x * 38094, AWAT2, sequence calculation
38145
x * 38145, AWAT2, sequence calculation
38536
-
x * 38599, AWAT1, sequence calculation, x * 38536, AWAT2, sequence calculation
38599
-
x * 38599, AWAT1, sequence calculation, x * 38536, AWAT2, sequence calculation
40000
gel filtration
41200
x * 41200, calculated
53000
2 * 53000, SDS-PAGE
94100
gel filtration
additional information
amino acid sequence analysis and alignment
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 53000, SDS-PAGE
additional information
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
reduced stability
50
-
10 min, complete inactivation
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
no improvement of heat-stability by polyvinylpyrrolidone
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, several months without significant loss of activity
0°C, fairly stable
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4°C, 2-3 h stable
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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
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recombinant soluble N-terminally His-tagged enzyme 19.2fold from Escherichia coli strain BL21(DE3) by cation exchange and nickel affinity chromatography
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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)
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expression in Escherichia coli
expression in Saccharomyces cerevisiae
expression in Saccharomyces cerevisiae and Escherichia coli
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functional expression in Escherichia coli strain BL21(DE3)
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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
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gene atfA, expression of wild-type and mutant enzymes in Escherichia coli strain Rosetta(DE3)
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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)
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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
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screening, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain JM109
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D137A
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the mutant shows slightly reduced activity compared to the wild-type enzyme
G138A
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the mutant shows slightly reduced activity compared to the wild-type enzyme
G355I
Q8GG1
mutation improves the rate of reaction
H132L
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the replacement of His132 leads to reduced enzyme activity
H132L/H133L
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inactive mutant
H133L
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the replacement of His133 leads to highly reduced enzyme activity
A360F
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mutation slightly improves the rate of reaction found for smaller fatty alcohols
A360I
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mutation improves the rate of reaction found for smaller fatty alcohols
A360V
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mutation improves the rate of reaction found for smaller fatty alcohols
L356A
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mutation increases selectivity toward ethanol
L356F
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mutation increases selectivity toward ethanol, with a drop in specific activity of approximately 89% for dodecanol
L356V
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mutation increases selectivity toward 2-phenylethanol
L356Y
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substantial loss of activity
M405A
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significant decrease in overall activity with dodecanol
M405F
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mutation increases selectivity toward isoamyl alcohol, significant decrease in overall activity with dodecanol
M405L
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significant decrease in overall activity with dodecanol
M405W
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dramatically shifts selectivity toward ethanol, significant decrease in overall activity with dodecanol
A360F
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mutation slightly improves the rate of reaction found for smaller fatty alcohols
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A360I
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mutation improves the rate of reaction found for smaller fatty alcohols
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A360V
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mutation improves the rate of reaction found for smaller fatty alcohols
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L356A
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mutation increases selectivity toward ethanol
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L356F
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mutation increases selectivity toward ethanol, with a drop in specific activity of approximately 89% for dodecanol
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L356V
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mutation increases selectivity toward 2-phenylethanol
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L356Y
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substantial loss of activity
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M405F
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mutation increases selectivity toward isoamyl alcohol, significant decrease in overall activity with dodecanol
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N36R
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mutant enzyme is capable of synthesizing very long chain fatty acyl-harboring wax esters
additional information
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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Show AA Sequence (110 entries)
Please use the Sequence Search for a specific query.
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.1.75)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)