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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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.
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
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
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
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
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
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
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
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
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