. 2003 Nov;133(3):1306–1313. doi: 10.1104/pp.103.025213

Table III.

Substrate specificity of the leachianone G 2″-dimethylallyltransferase activity

Substrate (Donor)	Relative Activity	Substrate (Acceptor)	Relative Activity
	%		%
DMAPP	100 ± 3.0^a	Leachianone G	100 ± 3.0^a
IPP	n.d.^b	Euchrenone a₇	54 ± 1.5^c
GPP	n.d.	Kenusanone I	n.i.^d
		8-Dimethylallylnaringenin	n.d.
		Isovabachin	n.d.

The ultimate concentrations of acceptors and donors are 0.3 mM and 1 mM, respectively. Structures of acceptors were shown below (for leachianone G, see Fig. 1). The HPLC assay were performed according to the standard method described in “Materials and Methods”. Data are means of duplicate determinations ± se.

^a LGDT activity was 41.1 pkat mg protein-1.

^b Compared with heat-denatured control assay, any additional peaks were not detected.

^c The prenylated product was identified as lehmannin by comparison with authentic lehmannin using HPLC photodiode-array analysis.

^d The production of new compound, the elution profile of which was resemble to that of the expected product was observed (in the present HPLC condition, 8-lavandulyated product was eluted ca. 6 min later than 8-dimethylallylated substrate), though was not identified. Conversion rate of it was 11 ± 0.3 (% of control).