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Information on EC 2.3.1.75 - long-chain-alcohol O-fatty-acyltransferase and Organism(s) Mus musculus and UniProt Accession Q6E1M8
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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
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arats
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biodiesels
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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: Mus musculus
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, wax ester synthase/diacylglycerol acyltransferase, atfa1, wax ester synthase/acyl-coenzyme a:diacylglycerol acyltransferase, maqu_0168, acyl-coa wax alcohol acyltransferases, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acyltransferase, long-chain alcohol
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wax synthase
wax-ester synthase
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additional information
wax synthase
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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
myristoyl-CoA + 11-cis-retinol
11-cis-retinyl myristate + CoA
preferred substrate
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myristoyl-CoA + all-trans-retinol
all-trans-retinyl myristate + CoA
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?
additional information
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prefers monounsaturated and polyunsaturated C18:1 and C18:2 fatty alcohols over C18:0, and prefers 20:1 fatty alcohol over C20:0. Enzyme prefers shorter chain fatty acyl-CoA substrates and does not discriminate between monounsaturated and polyunsaturated fatty acyl CoA substrates. Enzyme also uses 10, 15, and 20 carbon isoprenoid alcohols
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additional information
?
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prefers monounsaturated and polyunsaturated C18:1 and C18:2 fatty alcohols over C18:0, and prefers 20:1 fatty alcohol over C20:0. Enzyme prefers shorter chain fatty acyl-CoA substrates and does not discriminate between monounsaturated and polyunsaturated fatty acyl CoA substrates. Enzyme also uses 10, 15, and 20 carbon isoprenoid alcohols
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additional information
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the 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
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additional information
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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
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additional information
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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
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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
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AWAT2_MOUSE
333
1
38145
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
predicted secondary and transmembrane structures of isozyme AWAT2, overview
additional information
predicted secondary and transmembrane structures of isozyme AWAT2, overview
additional information
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predicted secondary and transmembrane structures of isozyme AWAT2, overview
additional information
predicted secondary and transmembrane structures of isozyme AWAT1, overview
additional information
predicted secondary and transmembrane structures of isozyme AWAT1, overview
additional information
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predicted secondary and transmembrane structures of isozyme AWAT1, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N36R
mutant enzyme is capable of synthesizing very long chain fatty acyl-harboring wax esters
additional information
additional information
domain swap experiment between the mouse acyl-CoA:wax alcohol acyltransferase (AWAT2) and the homologous mouse acyl-CoA:diacylglycerol O-acyltransferase 2 (DGAT2). Te substrate specificity of AWAT2 is partially determined by two predicted transmembrane domains near the amino terminus of AWAT2. Upon exchange of the two domains for the respective part of DGAT2, the resulting chimeric enzyme is capable of incorporating up to 20% of very long acyl chains in the wax esters upon expression in Saccharomyces cerevisiae. The amount of very long acyl chains in wax esters synthesized by wild type AWAT2 is negligible. The effect is due to a single amino acid exchange within one of the predicted membrane domains, the AWAT2 N36R
additional information
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domain swap experiment between the mouse acyl-CoA:wax alcohol acyltransferase (AWAT2) and the homologous mouse acyl-CoA:diacylglycerol O-acyltransferase 2 (DGAT2). Te substrate specificity of AWAT2 is partially determined by two predicted transmembrane domains near the amino terminus of AWAT2. Upon exchange of the two domains for the respective part of DGAT2, the resulting chimeric enzyme is capable of incorporating up to 20% of very long acyl chains in the wax esters upon expression in Saccharomyces cerevisiae. The amount of very long acyl chains in wax esters synthesized by wild type AWAT2 is negligible. The effect is due to a single amino acid exchange within one of the predicted membrane domains, the AWAT2 N36R
additional information
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the wax diester synthase activity of DGAT1 helps to explain the deficiency of type II wax diesters in the fur lipids of Dgat-/- mice
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose column chromatography and Superdex S200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozyme AWAT2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
isozyme AWAT1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cheng, J.B.; Russell, D.W.
Mammalian wax biosynthesis. II. Expression cloning of wax synthase cDNAs encoding a member of the acyltransferase enzyme family
J. Biol. Chem.
279
37798-37807
2004
Homo sapiens (Q6E213), Mus musculus (Q6E1M8), Mus musculus
Yen, C.L.; Monetti, M.; Burri, B.J.; Farese, R.V.
The triacylglycerol synthesis enzyme DGAT1 also catalyzes the synthesis of diacylglycerols, waxes, and retinyl esters
J. Lipid Res.
46
1502-1511
2005
Mus musculus
Holmes, R.
Comparative genomics and proteomics of vertebrate diacylglycerol acyltransferase (DGAT), acyl CoA wax alcohol acyltransferase (AWAT) and monoacylglycerol acyltransferase (MGAT)
Comp. Biochem. Physiol. D
5
45-54
2010
Homo sapiens (Q58HT5), Homo sapiens (Q6E213), Homo sapiens, Monodelphis domestica, Mus musculus (A2ADU9), Mus musculus (Q6E1M8), Mus musculus
Miklaszewska, M.; Kawinski, A.; Banas, A.
Detailed characterization of the substrate specificity of mouse wax synthase
Acta Biochim. Pol.
60
209-215
2013
Mus musculus (Q6E1M8), Mus musculus
Kawelke, S.; Feussner, I.
Two predicted transmembrane domains exclude very long chain fatty acyl-CoAs from the active site of mouse wax synthase
PLoS ONE
10
e0145797
2015
Mus musculus (Q6E1M8), Mus musculus
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