taxonID	type	format	identifier	references	title	description	created	creator	contributor	publisher	audience	source	license	rightsHolder	datasetID
03AD87AFFFF8FFB5120FFDB23C39FA3A.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8291068/files/figure.png	https://doi.org/10.5281/zenodo.8291068	Fig. 1. a, The proposed reaction mechanism for the synthesis of limonene, pinene and sabinene. b, The structural model of pinene synthase docked with the terpinyl (left), pinyl (middle) and thujyl (right) cations. Carbocations are colored in magenta (terpinyl), wheat (pinyl) and cyan (thujyl). Other atoms are colored according to their types (red: oxygen; yellow: carbon; blue: nitrogen; orange: phosphorus; green: magnesium). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)	Fig. 1. a, The proposed reaction mechanism for the synthesis of limonene, pinene and sabinene. b, The structural model of pinene synthase docked with the terpinyl (left), pinyl (middle) and thujyl (right) cations. Carbocations are colored in magenta (terpinyl), wheat (pinyl) and cyan (thujyl). Other atoms are colored according to their types (red: oxygen; yellow: carbon; blue: nitrogen; orange: phosphorus; green: magnesium). (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)	2021-01-31	Xu, Jingwei;Peng, Guanzu;Xu, Jinkun;Li, Yi;Tong, Li;Yang, Dong		Zenodo	biologists	Xu, Jingwei;Peng, Guanzu;Xu, Jinkun;Li, Yi;Tong, Li;Yang, Dong			
03AD87AFFFF8FFB5120FFDB23C39FA3A.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8291070/files/figure.png	https://doi.org/10.5281/zenodo.8291070	Fig. 2. Converting pinene synthase to sabinene synthase by mutations on 482 position. Chromatograms in a, b, c, d and e show the GC-MS analysis of terpene products for WT, F482A, F482I, F482V and F482T, respectively. The x-axis is the retention time and the y-axis is the relative abundance of each species. The numbers in each peak correspond to α-pinene (1), sabinene (2) and limonene (3).	Fig. 2. Converting pinene synthase to sabinene synthase by mutations on 482 position. Chromatograms in a, b, c, d and e show the GC-MS analysis of terpene products for WT, F482A, F482I, F482V and F482T, respectively. The x-axis is the retention time and the y-axis is the relative abundance of each species. The numbers in each peak correspond to α-pinene (1), sabinene (2) and limonene (3).	2021-01-31	Xu, Jingwei;Peng, Guanzu;Xu, Jinkun;Li, Yi;Tong, Li;Yang, Dong		Zenodo	biologists	Xu, Jingwei;Peng, Guanzu;Xu, Jinkun;Li, Yi;Tong, Li;Yang, Dong			
03AD87AFFFF8FFB5120FFDB23C39FA3A.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8291072/files/figure.png	https://doi.org/10.5281/zenodo.8291072	Fig. 3. Hybrid quadrupole-orbitrap GC-MS/MS. a shows the chromatogram of terpene products of F482L. The elution peak corresponding to sabinene is labeled. The mass spectrum of the product eluted at 9.29 min from a is shown in b. The mass spectrum of the standard sabinene is shown in c.	Fig. 3. Hybrid quadrupole-orbitrap GC-MS/MS. a shows the chromatogram of terpene products of F482L. The elution peak corresponding to sabinene is labeled. The mass spectrum of the product eluted at 9.29 min from a is shown in b. The mass spectrum of the standard sabinene is shown in c.	2021-01-31	Xu, Jingwei;Peng, Guanzu;Xu, Jinkun;Li, Yi;Tong, Li;Yang, Dong		Zenodo	biologists	Xu, Jingwei;Peng, Guanzu;Xu, Jinkun;Li, Yi;Tong, Li;Yang, Dong			
03AD87AFFFF8FFB5120FFDB23C39FA3A.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8291077/files/figure.png	https://doi.org/10.5281/zenodo.8291077	Fig. 4. Conformational differences in the pinyl cation in WT and F482Y as demonstrated by molecular dynamics simulation. The structures of WT and F482Y are superimposed. Results after 0, 1 and 2 ns of simulation are shown in a, d and c, respectively. Carbon in WT is colored in yellow and carbon in F482Y is colored in green. Oxygen is colored in red. Nitrogen is colored in blue. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)	Fig. 4. Conformational differences in the pinyl cation in WT and F482Y as demonstrated by molecular dynamics simulation. The structures of WT and F482Y are superimposed. Results after 0, 1 and 2 ns of simulation are shown in a, d and c, respectively. Carbon in WT is colored in yellow and carbon in F482Y is colored in green. Oxygen is colored in red. Nitrogen is colored in blue. (For interpretation of the references to color in this figure legend, the reader is referred to the Web version of this article.)	2021-01-31	Xu, Jingwei;Peng, Guanzu;Xu, Jinkun;Li, Yi;Tong, Li;Yang, Dong		Zenodo	biologists	Xu, Jingwei;Peng, Guanzu;Xu, Jinkun;Li, Yi;Tong, Li;Yang, Dong			
03AD87AFFFF8FFB5120FFDB23C39FA3A.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8291079/files/figure.png	https://doi.org/10.5281/zenodo.8291079	Fig. 5. The effect of the S491A mutation. Chromatograms in a, b and c show the GC-MS analysis of terpene production for S491A, F482A/S491A, and F482I/S491A, respectively. The x-axis is the retention time and the y-axis is the relative abundance of each species. The numbers in each peak correspond to α-pinene (1), sabinene (2) and limonene (3). d shows the overall activity and the percentage of sabinene within total products produced by F482A, F482A/S491A, F482I and F482I/S491A. The asterisk indicates P <0.05.	Fig. 5. The effect of the S491A mutation. Chromatograms in a, b and c show the GC-MS analysis of terpene production for S491A, F482A/S491A, and F482I/S491A, respectively. The x-axis is the retention time and the y-axis is the relative abundance of each species. The numbers in each peak correspond to α-pinene (1), sabinene (2) and limonene (3). d shows the overall activity and the percentage of sabinene within total products produced by F482A, F482A/S491A, F482I and F482I/S491A. The asterisk indicates P <0.05.	2021-01-31	Xu, Jingwei;Peng, Guanzu;Xu, Jinkun;Li, Yi;Tong, Li;Yang, Dong		Zenodo	biologists	Xu, Jingwei;Peng, Guanzu;Xu, Jinkun;Li, Yi;Tong, Li;Yang, Dong			
03AD87AFFFF8FFB5120FFDB23C39FA3A.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8291081/files/figure.png	https://doi.org/10.5281/zenodo.8291081	Fig. 6. S491A mutation increases the rigidity of the active pocket when it binds the pinyl cation. RMSD values of the active site residues between WT and S491A in complex with the pinyl cation (a), terpinyl cation (b) and thujyl cation (c) are compared.	Fig. 6. S491A mutation increases the rigidity of the active pocket when it binds the pinyl cation. RMSD values of the active site residues between WT and S491A in complex with the pinyl cation (a), terpinyl cation (b) and thujyl cation (c) are compared.	2021-01-31	Xu, Jingwei;Peng, Guanzu;Xu, Jinkun;Li, Yi;Tong, Li;Yang, Dong		Zenodo	biologists	Xu, Jingwei;Peng, Guanzu;Xu, Jinkun;Li, Yi;Tong, Li;Yang, Dong			
03AD87AFFFF8FFB5120FFDB23C39FA3A.taxon	http://purl.org/dc/dcmitype/StillImage	image/png	https://zenodo.org/record/8291083/files/figure.png	https://doi.org/10.5281/zenodo.8291083	Fig. 7. The RMSD profiles of the region with high (RMSD H) and low (RMSD L) mobility from the simulation of WT (a), S491A (b) and F482/S491A (c) in complex with the pinyl cation.	Fig. 7. The RMSD profiles of the region with high (RMSD H) and low (RMSD L) mobility from the simulation of WT (a), S491A (b) and F482/S491A (c) in complex with the pinyl cation.	2021-01-31	Xu, Jingwei;Peng, Guanzu;Xu, Jinkun;Li, Yi;Tong, Li;Yang, Dong		Zenodo	biologists	Xu, Jingwei;Peng, Guanzu;Xu, Jinkun;Li, Yi;Tong, Li;Yang, Dong			
