Fig. 4: Structural comparison of CrLAMT and CaLAMT and enzyme activity assay. | Nature Communications

Fig. 4: Structural comparison of CrLAMT and CaLAMT and enzyme activity assay.

From: A chromosome-level Camptotheca acuminata genome assembly provides insights into the evolutionary origin of camptothecin biosynthesis

Fig. 4

a Structures of CrLAMT and CaLAMT and their ligand binding energies calculated by AutoDock. b Docking results for loganic acid. Blue indicates hydrogen bonds while red indicates binding sites with mutations in CaLAMT compared with CrLAMT. c Phylogenetic relationship and protein sequence alignment of CrLAMT, CaLAMT, and LAMT homologs from other species. Binding sites and regions are shown in blue while sites with mutations are shown in red. RtLAMT: loganic acid O-methyltransferase from Rauvolfia tetraphyla; SsLAMT: loganic acid O-methyltransferase from Strychnos spinosa; OpLAMT: loganic acid O-methyltransferase from Ophiorrhiza pumila; LjLAMT: loganic acid O-methyltransferase from Lonicera japonica; MtLAMT: loganic acid O-methyltransferase from Menyanthes trifoliata. d Relative activities of CrLAMT WT, CaLAMT WT and the mutated CrLAMT compared to those found in CaLAMT. Relative enzyme activity was calculated using CrLAMT WT as a reference (n = 3 independent experiments for each enzyme). Significance was tested by a two-tailed unpaired t-test method (error bars, mean ± s.d) with asterisks indicating p-value (***p < 0.001; **p < 0.01; *p < 0.05). Source data underlying Fig. 4d are provided as a Source Data file.

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