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Information on EC 2.3.1.20 - diacylglycerol O-acyltransferase and Organism(s) Acinetobacter baylyi and UniProt Accession Q8GGG1

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EC Tree
IUBMB Comments
Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
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This record set is specific for:
Acinetobacter baylyi
UNIPROT: Q8GGG1
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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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
DGAT1
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DGAT1A
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DGAT2
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DGAT2A
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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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:1,2-diacyl-sn-glycerol O-acyltransferase
Palmitoyl-CoA and other long-chain acyl-CoAs can act as donors.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-98-5
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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
palmitoyl-CoA + 1,2-dipalmitin
CoA + tripalmitin
show the reaction diagram
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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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?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
protein is mainly localised on the cytoplasmic site of the plasma membrane and on the surface of intracellular wax ester inclusions
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47400
deduced from cDNA
97000
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
total loss of activity at temperatures above 65°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, without significant loss of its activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
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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Manually annotated by BRENDA team