Localization of cinnamic acid 4-Monooxygenase and the membrane-bound enzyme system for dhurrin biosynthesis in sorghum seedlings

Saunders , J.A. and Conn, E.E. and Lin , C.H. and Shimada, M. (1977) Localization of cinnamic acid 4-Monooxygenase and the membrane-bound enzyme system for dhurrin biosynthesis in sorghum seedlings. Plant Physiology, 60 (4). pp. 629-634.

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Abstract

The localization of three monooxygenase (hydroxylase) enzyme systems which occur in dark-grown seedlings of Sorghum bicolor has been studied. Cinnamic acid 4-hydroxylase (CAH) (trans-cinnamate 4-monooxygenase, EC 1.14.13.11), which has been increasingly utilized in plants as a marker for the endoplasmic reticulum, migrated with that fraction in continuous and discontinuous sucrose gradients. When 10 mm MgCl2 was used to shift the density banding of the marker enzyme, NADPH cytochrome c reductase, from 1.12 to 1.17 g/cm3, the CAH activity was displaced as well. The membrane-bound enzyme system involved in the biosynthesis of the cyanogenic glucoside dhurrin was also shown to be closely associated with the endoplasmic reticulum. This system contains hydroxylases capable of hydroxylating tyrosine to form N-hydroxytyrosine and hydroxylating p-hydroxyphenylacetonitrile to form p-hydroxy-(S)-mandelonitrile

Item Type: Article
Author Affiliation: Department of Biochemistry and Biophysics, University of California, Davis, California 95616
Subjects: Plant Physiology and Biochemistry > Plant Physiology
Plant Physiology and Biochemistry > Biochemistry
Divisions: Sorghum
Depositing User: Ms K Syamalamba
Date Deposited: 10 Oct 2012 05:32
Last Modified: 10 Oct 2012 05:32
Official URL: http:/​/​dx.​doi.​org/​10.​1104/​pp.​60.​4.​629
URI: http://eprints.icrisat.ac.in/id/eprint/8352

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