Published June 30, 2021
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Fig. 5 in Anthocyanin 5,3 -aromatic acyltransferase from Gentiana triflora, a structural insight into biosynthesis of a blue anthocyanin
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- 1. Division of Biomedical Measurements and Diagnostics, Graduate School of Biomedical Engineering, Tohoku University, Sendai, 980-8575, Japan & * & Laboratory for Protein Functional and Structural Biology, RIKEN Center for Biosystems Dynamics Research, Yokohama, 230-0045, Japan
Description
Fig. 5. Summary of key amino acids for acyl-CoA specificity. The acyl-CoA binding pocket is illustrated with gray elongated semicircles. The upper and lower parts are binding pockets for malonyl/acetyl-CoA and caffeoyl/ coumaroyl-CoA, respectively. Four critical positions for acyl-CoA selectivity are indicated by blue ellipse. In the vicinity of these amino acid positions, the enzymes which have corresponding amino acid(s) are listed. The malonyl-CoA selective enzymes possess either Arg at the position 45/182, Val at the position 179, or Asp/Trp at the position 401 (upper part). In contrast, the caffeoyl/ coumaroyl-CoA selective enzymes have Ala/Gly at the position 179 and Gly/ Ser at the position 401 and include Arg neither at the position 45 nor 182 (lower part). PDB-ID is indicated in parentheses for enzymes with known structure. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)
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- Is part of
- Journal article: 10.1016/j.phytochem.2021.112727 (DOI)
- Journal article: urn:lsid:plazi.org:pub:FF8FE33AFFE2E70A0D7DD21AFFDBFFE9 (LSID)
- Journal article: https://zenodo.org/record/8258615 (URL)