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Literature summary extracted from

  • 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 (2007), Biochimie, 89, 230-242.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.20 expressed in Escherichia coli Mycolicibacterium smegmatis
2.3.1.20 expressed in Escherichia coli Streptomyces avermitilis
2.3.1.20 expressed in Escherichia coli Acinetobacter baylyi
2.3.1.20 expressed in Escherichia coli Mycobacterium tuberculosis
2.3.1.20 expressed in Escherichia coli Streptomyces coelicolor
2.3.1.75 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 Acinetobacter baylyi
2.3.1.75 genes with high homologies to the Acinetobacter sp. ADP1 atfA are identified in the genome databases of several Gram-negative strains, including marine bacteria like Hahella chejuensis, psychrophilic strains like Psychrobacter sp., Polaromonas sp. and Bradyrhizobium japonicum. Ten atfA homologous genes are identified in the genome database of Arabidopsis thaliana Acinetobacter baylyi ADP1

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.20 additional information construction of a SCO0958 deletion mutant shows that the protein is responsible for biosynthesis of a significant amount of triacylglycerol Streptomyces coelicolor
2.3.1.20 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 Acinetobacter baylyi
2.3.1.75 additional information construction of knockout mutants by transposon mutagenesis Acinetobacter baylyi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.20 0.026
-
 oleoyl-CoA
-
 Mycobacterium tuberculosis
2.3.1.20 0.028
-
 diolein
-
 Mycobacterium tuberculosis
2.3.1.20 0.667
-
 oleoyl-CoA
-
 Mycobacterium tuberculosis
2.3.1.20 0.714
-
 diolein
-
 Mycobacterium tuberculosis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.20 membrane protein is mainly localised on the cytoplasmic site of the plasma membrane and on the surface of intracellular wax ester inclusions Acinetobacter baylyi 16020
-
2.3.1.75 lipid body
-
 Acinetobacter baylyi
-
-
2.3.1.75 membrane
-
 Acinetobacter baylyi ADP1 16020
-
2.3.1.75 membrane
-
 Acinetobacter baylyi 16020
-
2.3.1.75 additional information the enzyme exhibits a very specific adsorption pattern to artificial phospholipid membranes Acinetobacter baylyi
-
-
2.3.1.75 plasma membrane 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 Acinetobacter baylyi 5886
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.20 30800
-
 deduced from cDNA Mycobacterium tuberculosis
2.3.1.20 47100
-
 deduced from cDNA Streptomyces coelicolor
2.3.1.20 47400
-
 deduced from cDNA Streptomyces avermitilis
2.3.1.20 47400
-
 deduced from cDNA Acinetobacter baylyi
2.3.1.20 49300
-
 deduced from cDNA Mycobacterium tuberculosis
2.3.1.20 49600
-
 Wdh3563-2 deduced from cDNA Mycolicibacterium smegmatis
2.3.1.20 49900
-
 Wdh3563-4 deduced from cDNA Mycolicibacterium smegmatis
2.3.1.20 50200
-
 Wdh3563-1 deduced from cDNA Mycolicibacterium smegmatis
2.3.1.20 50700
-
 deduced from cDNA Mycobacterium tuberculosis
2.3.1.20 50900
-
 deduced from cDNA Mycobacterium tuberculosis
2.3.1.20 51600
-
 Wdh3563-7 deduced from cDNA Mycolicibacterium smegmatis
2.3.1.20 51900
-
 Wdh3563-3 deduced from cDNA Mycolicibacterium smegmatis
2.3.1.20 97000
-
 gel filtration Acinetobacter baylyi
2.3.1.75 51800
-
 x * 51800, calculated from sequence Acinetobacter baylyi ADP1

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.75 additional information Acinetobacter baylyi key enzyme in the biosynthesis of neutral lipid storage compounds, triacylglycerols and wax esters, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.20 Acinetobacter baylyi Q8GGG1
-
-
2.3.1.20 Mycobacterium tuberculosis P9WKC3
-
-
2.3.1.20 Mycobacterium tuberculosis P9WKC5
-
-
2.3.1.20 Mycobacterium tuberculosis P9WKC7
-
-
2.3.1.20 Mycobacterium tuberculosis P9WKC9
-
-
2.3.1.20 Mycobacterium tuberculosis H37Rv P9WKC3
-
-
2.3.1.20 Mycobacterium tuberculosis H37Rv P9WKC5
-
-
2.3.1.20 Mycobacterium tuberculosis H37Rv P9WKC7
-
-
2.3.1.20 Mycobacterium tuberculosis H37Rv P9WKC9
-
-
2.3.1.20 Mycolicibacterium smegmatis
-
-
-
2.3.1.20 Streptomyces avermitilis Q826D7
-
-
2.3.1.20 Streptomyces coelicolor Q9RIU8
-
-
2.3.1.75 Acinetobacter baylyi
-
 i.e. Acinetobacter calcoaceticus, strain ADP1
-
2.3.1.75 Acinetobacter baylyi ADP1 Q8GGG1 bifunctional protein
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.20 purified enzyme is obtained by cation exchange chromatography, hydrophobic interaction chromatography and subsequent ion exchange chromatography Acinetobacter baylyi
2.3.1.75 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 Acinetobacter baylyi

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.75 acyl-CoA + a long-chain alcohol = CoA + a long-chain ester reaction mechanism Acinetobacter baylyi
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.20 additional information
-
 does not show any DGAT activity when expressed in recombinant Escherichia coli Streptomyces coelicolor
2.3.1.20 additional information
-
 high DGAT activity when expressed in recombinant Escherichia coli Mycobacterium tuberculosis
2.3.1.20 additional information
-
 shows DGAT activity when expressed in recombinant Escherichia coli Mycolicibacterium smegmatis
2.3.1.20 additional information
-
 shows DGAT activity when expressed in recombinant Escherichia coli Streptomyces avermitilis
2.3.1.20 0.3
-
-
 Acinetobacter baylyi
2.3.1.75 0.275
-
 purified His-tagged recombinant enzyme, with palmitoyl-CoA Acinetobacter baylyi

Storage Stability

EC Number Storage Stability Organism
2.3.1.20 -70°C, without significant loss of its activity Acinetobacter baylyi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.20 additional information 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 Acinetobacter baylyi ?
-
 ?
2.3.1.20 oleoyl-CoA + diolein
-
 Mycobacterium tuberculosis CoA + triolein
-
 ?
2.3.1.20 oleoyl-CoA + diolein
-
 Mycobacterium tuberculosis H37Rv CoA + triolein
-
 ?
2.3.1.75 acyl-CoA + long-chain diacylglycerol
-
 Acinetobacter baylyi CoA + long-chain triacylglycerol
-
 ?
2.3.1.75 acyl-CoA + long-chain fatty alcohol
-
 Acinetobacter baylyi CoA + long-chain fatty ester
-
 ?
2.3.1.75 additional information key enzyme in the biosynthesis of neutral lipid storage compounds, triacylglycerols and wax esters, overview Acinetobacter baylyi ?
-
 ?
2.3.1.75 additional information a bifunctional enzyme also catalyzing the reaction of EC 2.3.1.20 Acinetobacter baylyi ?
-
 ?
2.3.1.75 palmitoyl-CoA + long-chain fatty alcohol
-
 Acinetobacter baylyi CoA + long-chain palmitoyl ester
-
 ?

Subunits

EC Number Subunits Comment Organism
2.3.1.20 homodimer
-
 Acinetobacter baylyi
2.3.1.75 ? x * 51800, calculated from sequence Acinetobacter baylyi ADP1
2.3.1.75 More 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 Acinetobacter baylyi

Synonyms

EC Number Synonyms Comment Organism
2.3.1.20 AtfA enzyme possesses both wax ester synthase and diacylglycerol:acyl-coenzyme A acyltransferase (DGAT) activities Acinetobacter baylyi
2.3.1.20 DGAT
-
 Mycolicibacterium smegmatis
2.3.1.20 DGAT
-
 Streptomyces avermitilis
2.3.1.20 DGAT
-
 Acinetobacter baylyi
2.3.1.20 DGAT
-
 Mycobacterium tuberculosis
2.3.1.20 DGAT
-
 Streptomyces coelicolor
2.3.1.20 diacylglycerol acyltransferase
-
 Mycolicibacterium smegmatis
2.3.1.20 diacylglycerol acyltransferase
-
 Streptomyces avermitilis
2.3.1.20 diacylglycerol acyltransferase
-
 Acinetobacter baylyi
2.3.1.20 diacylglycerol acyltransferase
-
 Mycobacterium tuberculosis
2.3.1.20 diacylglycerol acyltransferase
-
 Streptomyces coelicolor
2.3.1.20 Rv3088 (TGS4)
-
 Mycobacterium tuberculosis
2.3.1.20 Rv3130c (TGS1)
-
 Mycobacterium tuberculosis
2.3.1.20 Rv3234c (TGS3)
-
 Mycobacterium tuberculosis
2.3.1.20 Rv3734 (TGS2)
-
 Mycobacterium tuberculosis
2.3.1.20 SAV7256 enzyme possesses both wax ester synthase and diacylglycerol:acyl-coenzyme A acyltransferase (DGAT) activities Streptomyces avermitilis
2.3.1.20 SCO0958
-
 Streptomyces coelicolor
2.3.1.20 TAG synthase
-
 Mycobacterium tuberculosis
2.3.1.20 Wdh3563-1
-
 Mycolicibacterium smegmatis
2.3.1.20 Wdh3563-2
-
 Mycolicibacterium smegmatis
2.3.1.20 Wdh3563-3
-
 Mycolicibacterium smegmatis
2.3.1.20 Wdh3563-4
-
 Mycolicibacterium smegmatis
2.3.1.20 Wdh3563-7
-
 Mycolicibacterium smegmatis
2.3.1.75 AtfA
-
 Acinetobacter baylyi ADP1
2.3.1.75 AtfA
-
 Acinetobacter baylyi
2.3.1.75 More cf. EC 2.3.1.20, the enzyme belongs to the WS/DGAT family Acinetobacter baylyi
2.3.1.75 wax ester synthases/acyl-CoA:diacylglycerol acyltransferase
-
 Acinetobacter baylyi ADP1
2.3.1.75 WE synthases/acyl-CoA:diacylglycerol acyltransferase
-
 Acinetobacter baylyi
2.3.1.75 WS/DGAT
-
 Acinetobacter baylyi ADP1
2.3.1.75 WS/DGAT
-
 Acinetobacter baylyi

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.3.1.20 40 45
-
 Acinetobacter baylyi

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.3.1.20 65
-
 total loss of activity at temperatures above 65°C Acinetobacter baylyi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.20 8
-
-
 Acinetobacter baylyi

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.3.1.20 6.5 7.2
-
 Mycobacterium tuberculosis

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.3.1.75 Acinetobacter baylyi ADP1 calculated from sequence
-
 9.05