Published November 3, 2018
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Fig. 5 in Genome-wide identification and biochemical characterization of the UGT88F subfamily in Malus x domestica Borkh
Description
Fig. 5. Amino-acid sequence alignment of UGT88F6 and UGT88F8. Black shading indicates divergent amino acids between sequences and light gray shading indicates additional sequences compared to others UGT subfamilies. Black boxes include residues of the acceptor binding pocket. Among them, the position of residues involved in interaction with acceptor substrate as observed on the elucidated VvGT1, UGT78K6 and UGT78G1 crystal structure are marked with (#). The H and D corresponds to the UGT conserved histidine catalytic and aspartate helper involved in deprotonation of hydroxy group prior glycosylated. The highly conserved PSPG motif is in a gray box and residues interacting with the sugar donor are marked with (*). Predicted secondary structure elements (β-strands and αhelices) are indicates under the sequences.
Notes
Published as part of Elejalde-Palmett, Carolina, Billet, Kévin, Lanoue, Arnaud, Craene, Johan-Owen De, Glévarec, Gaëlle, Pichon, Olivier, Clastre, Marc, Courdavault, Vincent, St-Pierre, Benoit, Giglioli-Guivarc'h, Nathalie, Bernonville, Thomas Dugé de & Besseau, Sébastien, 2019, Genome-wide identification and biochemical characterization of the UGT88F subfamily in Malus x domestica Borkh, pp. 135-144 in Phytochemistry 157 on page 140, DOI: 10.1016/j.phytochem.2018.10.019, http://zenodo.org/record/10481366
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- Journal article: 10.1016/j.phytochem.2018.10.019 (DOI)
- Journal article: urn:lsid:plazi.org:pub:97163906FF87FFC8FFB6FFE8FFC5FFE7 (LSID)
- Journal article: http://publication.plazi.org/id/97163906FF87FFC8FFB6FFE8FFC5FFE7 (URL)
- Journal article: https://zenodo.org/record/10481366 (URL)