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Literature summary extracted from

  • Liu, Q.; Siloto, R.M.; Snyder, C.L.; Weselake, R.J.
    Functional and topological analysis of yeast acyl-CoA:diacylglycerol acyltransferase 2, an endoplasmic reticulum enzyme essential for triacylglycerol biosynthesis (2011), J. Biol. Chem., 286, 13115-13126.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
2.3.1.20 F71A mutant retains more than 40% of wild-type activity Saccharomyces cerevisiae
2.3.1.20 H193A almost complete loss of activity Saccharomyces cerevisiae
2.3.1.20 H193E/G196S mutation to corresponding motif found in plant, abolishes enzymic activity Saccharomyces cerevisiae
2.3.1.20 H195A complete loss of activity Saccharomyces cerevisiae
2.3.1.20 L73A mutant retains more than 40% of wild-type activity Saccharomyces cerevisiae
2.3.1.20 additional information construction of N- and C-terminal truncation mutants N1(DELTA1-62), N2 (DELTA1-33), C1 (DELTA374-418), C2 (DELTA391-418), C3 (DELTA413-418), C4 (DELTA413-418, 413::A6). Mutant N1 lacking the entire hydrophilic N terminus presents minimal activity while maintaining a substantial expression level. Removal of the first 33 amino acid residues in the N-terminus, mutant N2, results in minor decrease in enzyme activity. Deletion of the last six amino acid residues from the C-terminus, mutant C3, causes a decrease in the enzyme activity of more than 80%. Deletion of the whole C-terminus, mutant C1, completely abolishes the enzyme activity and has a substantial impact on the protein accumulation. Mutant C2 lacking about half of the C-terminus, exhibits a complete loss of activity. In mutant C4, the last six amino acid residues are replaced with six alanine residues. This mutant retains similar activity and expression levels to C3. Deletion of the first putative TMD between residues 70 and 91 also results in the total loss of activity Saccharomyces cerevisiae
2.3.1.20 Y129A/F130A/P131A almost complete loss of activity Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.20 endoplasmic reticulum both the N and C termini are oriented toward the cytosol and have different catalytic roles. A highly conserved motif, 129YFP131, and a hydrophilic segment exclusive to yeast DGAT2 reside in a long endoplasmic reticulum luminal loop following the first transmembrane domain and play an essential role in enzyme catalysis. The strongly conserved residue His195 within the motif HPHG, which may play a role in the active site of DGAT2, is likely embedded in the membrane Saccharomyces cerevisiae 5783
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Organism

EC Number Organism UniProt Comment Textmining
2.3.1.20 Saccharomyces cerevisiae Q08650 isoform DGAT2
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Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.20 1,2-dioleoylglycerol + oleoyl-CoA
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 Saccharomyces cerevisiae triolein + CoA
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 ?

Synonyms

EC Number Synonyms Comment Organism
2.3.1.20 DGA1
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 Saccharomyces cerevisiae
2.3.1.20 DGAT2
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 Saccharomyces cerevisiae