Protein Variants | Comment | Organism |
---|---|---|
F71A | mutant retains more than 40% of wild-type activity | Saccharomyces cerevisiae |
H193A | almost complete loss of activity | Saccharomyces cerevisiae |
H193E/G196S | mutation to corresponding motif found in plant, abolishes enzymic activity | Saccharomyces cerevisiae |
H195A | complete loss of activity | Saccharomyces cerevisiae |
L73A | mutant retains more than 40% of wild-type activity | Saccharomyces cerevisiae |
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 |
Y129A/F130A/P131A | almost complete loss of activity | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
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 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | Q08650 | isoform DGAT2 | - |
Source Tissue | Comment | Organism | Textmining |
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Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1,2-dioleoylglycerol + oleoyl-CoA | - |
Saccharomyces cerevisiae | triolein + CoA | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DGA1 | - |
Saccharomyces cerevisiae |
DGAT2 | - |
Saccharomyces cerevisiae |