A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine). Activity is induced by wounding of the plant tissue .
The enzyme appears in viruses and cellular organisms
A cytochrome P-450 (heme-thiolate) protein. This enzyme catalyses a step in the pathway of abietic acid biosynthesis. The activity has been demonstrated in cell-free stem extracts of Abies grandis (grand fir) and Pinus contorta (lodgepole pine). Activity is induced by wounding of the plant tissue [2].
Substrates: activity is induced by wounding of the plant tissue reaching a maximum at 10 days after wounding with about a 7fold increase for the abietadiene hydroxylase Products: -
Substrates: this enzyme catalyzes a step in the pathway of abietic acid biosynthesis. Hydroxylation activity is maximally supported by NADPH, and NADH is less effective as reductant Products: -
Substrates: activity is induced by wounding of the plant tissue reaching a maximum at 10 days after wounding with about a 7fold increase for the abietadiene hydroxylase Products: -
Substrates: this enzyme catalyzes a step in the pathway of abietic acid biosynthesis. Hydroxylation activity is maximally supported by NADPH, and NADH is less effective as reductant Products: -
Diterpenoid resin acid biosynthesis in conifers: characterization of two cytochrome P450-dependent monooxygenases and an aldehyde dehydrogenase involved in abietic acid biosynthesis
Funk, C.; Lewinsohn, E.; Vogel, B.; Steele, C.; Croteau, R.
Regulation of oleoresinosis in grand fir (Abies grandis). Coordinate induction of monoterpene and diterpene cyclases and two cytochrome P450-dependent diterpenoid hydroxylases by stem wounding
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