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EC Tree
IUBMB Comments Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
The taxonomic range for the selected organisms is: Acinetobacter baylyi The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
dgat1, dgat2, dgat, diacylglycerol acyltransferase, diacylglycerol acyltransferase 1, diacylglycerol o-acyltransferase, dgat-1, monoacylglycerol acyltransferase, acyl-coa:diacylglycerol acyltransferase, diacylglycerol acyltransferase 2,
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1,2-diacylglycerol acyltransferase
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acyl-CoA:1,2-dioleoyl-sn-glycerol acyltransferase
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acyltransferase, diacylglycerol
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AtfA
enzyme possesses both wax ester synthase and diacylglycerol:acyl-coenzyme A acyltransferase (DGAT) activities
diacylglycerol acyltransferase
diglyceride acyltransferase
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diglyceride O-acyltransferase
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palmitoyl-CoA-sn-1,2-diacylglycerol acyltransferase
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wax ester synthase/acyl-CoA:diacylglycerol acyltransferase
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DGAT
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diacylglycerol acyltransferase
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diacylglycerol acyltransferase
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Acyl group transfer
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acyl-CoA:1,2-diacyl-sn-glycerol O-acyltransferase
Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
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palmitoyl-CoA + 1,2-dipalmitin
CoA + tripalmitin
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additional information
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ATfA exhibits a clear preference for the acylation of the sn-2 position of sn-1,2-dipalmitoylglycerol rather than the sn-2 position of sn-1,3-dipalmitoylglycerol
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SwissProt
brenda
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protein is mainly localised on the cytoplasmic site of the plasma membrane and on the surface of intracellular wax ester inclusions
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D137A
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highly conserved residue in acyltransferases, mutation does not result in a significant decrease of activity
G138A
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highly conserved residue in acyltransferases, mutation does not result in a significant decrease of activity
H132L
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highly conserved residue in acyltransferases, mutation results in strongly decreased activity
H132L/H133L
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highly conserved residues in acyltransferases
H133L
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highly conserved residue in acyltransferases, residue essential for catalytic activity
additional information
expression of atfA in a quadruple mutant of Saccharomyces cerevisiae, lacking own DGAT and steryl ester synthase activites by disrupted DGA1, LRO1, ARE1 and ARE2, restores triacylglycerol but not steryl ester biosynthesis and results in the formation and accumulation of fatty acid ethyl and isoamyl esters, indicating that also eukaryotic systems are suitable hosts for atfA expression
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65
total loss of activity at temperatures above 65°C
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-70°C, without significant loss of its activity
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cation-exchange chromatography, hydrophobic interaction chromatography, anion-exchange chromatography
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purified enzyme is obtained by cation exchange chromatography, hydrophobic interaction chromatography and subsequent ion exchange chromatography
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expressed in Escherichia coli
expressed in Escherichia coli
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expressed in Escherichia coli
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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
Mycolicibacterium smegmatis, Mycobacterium tuberculosis (P9WKC3), Mycobacterium tuberculosis (P9WKC5), Mycobacterium tuberculosis (P9WKC7), Mycobacterium tuberculosis (P9WKC9), Streptomyces avermitilis (Q826D7), Acinetobacter baylyi (Q8GGG1), Streptomyces coelicolor (Q9RIU8), Mycobacterium tuberculosis H37Rv (P9WKC3), Mycobacterium tuberculosis H37Rv (P9WKC5), Mycobacterium tuberculosis H37Rv (P9WKC7), Mycobacterium tuberculosis H37Rv (P9WKC9)
brenda
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
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