Characterization of ent-kaurene oxidase activity from Gibberella fujikuroi
作者： Philip J. Ashman , Alan Mackenzie , Peter M. Bramley
DOI: 10.1016/0304-4165(90)90027-T
关键词:
摘要: Cell extracts of wild-type and mutant strains Gibberella fujikuroi were assayed for kaurene oxidase activity, using ent-[3H]kaurene as the substrate. Extracts from strain SG78 exhibited highest specific used in subsequent experiments. The microsomal enzyme activity was solubilized with buffers or salt solutions at a concentration 400 mM. Both soluble preparations showed characteristic cytochrome P-450 spectra, ligand binding spectra substrate plant growth regulator, paclobutrazol, inhibition enzymic by carbon monoxide. addition 20% glycerol to extraction buffer stabilized some extent. Loss on storage accompanied conversion P-420. Michaelis-Menten kinetic parameters membrane-bound have been estimated, constants ent-kaurene paclobutrazol P-420 forms protein.
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