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Information on EC 2.3.1.75 - long-chain-alcohol O-fatty-acyltransferase and Organism(s) Acinetobacter baylyi and UniProt Accession Q8GGG1
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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
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retinyl
-
arats
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biodiesels
-
lubricant
- marinobacter
- jojoba
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retinol-binding
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3hretinol
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lecithin:retinol
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simmondsia
- faees
- aquaeolei
- synthesis
- baylyi
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acyl-coa-dependent
- hexadecanol
- analysis
- agriculture
The taxonomic range for the selected organisms is: Acinetobacter baylyi
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
acyl-coa:retinol acyltransferase, wax synthase, wax ester synthase, awat2, awat1, atfa1, wax ester synthase/diacylglycerol acyltransferase, maqu_0168, wax ester synthase/acyl-coenzyme a:diacylglycerol acyltransferase, acyl-coa wax alcohol acyltransferases, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyltransferase, long-chain alcohol
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wax synthase
wax-ester synthase
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additional information
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cf. EC 2.3.1.20, the enzyme belongs to the WS/DGAT family
wax synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acyl-CoA + a long-chain alcohol = CoA + a long-chain ester
reaction mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Acyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:long-chain-alcohol O-acyltransferase
Transfers saturated or unsaturated acyl residues of chain-length C18 to C20 to long-chain alcohols, forming waxes. The best acceptor is cis-icos-11-en-1-ol.
CAS REGISTRY NUMBER
COMMENTARY
64060-40-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acyl-CoA + long-chain diacylglycerol
CoA + long-chain triacylglycerol
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-
-
-
?
acyl-CoA + long-chain fatty alcohol
CoA + long-chain fatty ester
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-
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-
?
dodecanol + palmitoyl-CoA
dodecanyl palmitate + CoA
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best substrate
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-
?
palmitoyl-CoA + long-chain fatty alcohol
CoA + long-chain palmitoyl ester
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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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the enzyme has high preference for C18 substrates
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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
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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-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140
substrate nonan-1-ol, wild-type, 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
360
substrate nonan-1-ol, mutant G355I, 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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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
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the enzyme exhibits a very specific adsorption pattern to artificial phospholipid membranes
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
H133L
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the replacement of His133 leads to highly reduced enzyme activity
additional information
additional information
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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
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 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
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
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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
the enzyme can be used for oleyl oleate production in plant seed oil
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kalscheuer, R.; Stoeveken, T.; Luftmann, H.; Malkus, U.; Reichelt, R.; Steinbuechel, A.
Neutral lipid biosynthesis in engineered Escherichia coli: jojoba oil-like wax esters and fatty acid butyl esters
Appl. Environ. Microbiol.
72
1373-1379
2006
Acinetobacter baylyi
Waeltermann, M.; Stoeveken, T.; Steinbuechel, A.
Key enzymes for biosynthesis of neutral lipid storage compounds in prokaryotes: Properties, function and occurrence of wax ester synthases/acyl-CoA:diacylglycerol acyltransferases
Biochimie
89
230-242
2007
Acinetobacter baylyi, Acinetobacter baylyi ADP1 (Q8GGG1)
Stveken, T.; Kalscheuer, R.; Steinbchel, A.
Both histidine residues of the conserved HHXXXDG motif are essential for wax ester synthase/acyl-CoA:diacylglycerol acyltransferase catalysis
Eur. J. Lipid Sci. Technol.
111
112-119
2009
Acinetobacter baylyi
-
Barney, B.M.; Wahlen, B.D.; Garner, E.; Wei, J.; Seefeldt, L.C.
Differences in substrate specificities of five bacterial wax ester synthases
Appl. Environ. Microbiol.
78
5734-5745
2012
Acinetobacter baylyi, Marinobacter nauticus, Psychrobacter cryohalolentis, Psychrobacter cryohalolentis K5, Rhodococcus jostii
Barney, B.; Mann, R.; Ohlert, J.
Identification of a residue affecting fatty alcohol selectivity in wax ester synthase
Appl. Environ. Microbiol.
79
396-399
2013
Acinetobacter baylyi (Q8GGG1), Acinetobacter baylyi, Marinobacter nauticus (A1TX06), Marinobacter nauticus DSM 11845 (A1TX06)
Yu, D.; Hornung, E.; Iven, T.; Feussner, I.
High-level accumulation of oleyl oleate in plant seed oil by abundant supply of oleic acid substrates to efficient wax ester synthesis enzymes
Biotechnol. Biofuels
11
53
2018
Marinobacter nauticus, Acinetobacter baylyi (Q8GGG1), Acinetobacter baylyi ATCC 3305 (Q8GGG1)
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