Cinnamic acid 4-hydroxylase from gherkin tissues |
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Authors: | E.Ellen Billett Harry Smith |
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Affiliation: | Department of Physiology and Environmental Studies, University of Nottingham, School of Agriculture, Sutton Bonington, Loughborough, LE12 5RD, Leicestershire, U.K. |
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Abstract: | Homogenates from 4-day-old gherkin cotyledons and hypocotyls fractionated by sucrose density gradient centrifugation contain cinnamic acid 4-hydroxylase activity, the activity being highest in the endoplasmic reticulum fractions. These fractions also contain very low concentrations of cytochrome P450. Hydroxylase activity is dependent on NADPH and on molecular oxygen, is optimal at pH 7.5 and is inhibited by carbon monoxide. The enzyme is very sensitive to inhibition by 2-mercaptoethanol, but it is not inhibited by the product, p-coumaric acid. Further, its responses to various potential inhibitors are fairly typical of mixed function oxidases from other sources. |
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Keywords: | Cucurbitaceae gherkin endoplasmic reticulum mixed function oxygenase properties. |
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