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Biosynthesis of (—)-Kaurene in Cell-free Extracts of Immature Pea Seeds

Biosynthesis of (—)-Kaurene in Cell-free Extracts of Immature Pea Seeds Abstract Mevalonate-14C was incorporated into (—)-kaurene-14C in cell-free extracts of immature pea (Pisum sativum L.) seeds. The identification of 14C-product as (—)-kaurene was based on: A) comparison with authentic (—)-kaurene on thin-layer and gas-liquid chromatography; and B) oxidation of 14C-product and (—)-kaurene with osmium tetroxide to form the common derivative kaurane-16,17-diol. The enzyme system is heat labile and is dependent upon ATP and Mg2+ or Mn2-, with Mn2+ being a more effective activator than Mg2+. The reaction rate was proportional to enzyme concentration in reaction mixtures containing 0.45 to 1.8 mg protein n/ml, and was linear with time through 120 minutes in standard reaction mixtures. Enzyme preparations from immature seeds of tall and dwarf peas appeared to synthesize (—)-kaurene at the same rate. Synthesis of (—)-kaurene was readily inhibited by Amo-1618. (2-Chloroethyl)-trimethylammonium chloride (CCC) also inhibited (—)-kaurene synthesis; however, approximately 1000-fold higher concentrations of CCC were required to evoke the same percentages of inhibition as Amo-1618. 1 This investigation was supported in part by Grant GB-4613 from the National Science Foundation. This paper is part of a thesis to be presented by James D. Anderson to the Graduate School of Oregon State University in partial fulfillment of the requirements for the Ph.D. degree. This content is only available as a PDF. © 1967 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model) http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Physiology Oxford University Press

Biosynthesis of (—)-Kaurene in Cell-free Extracts of Immature Pea Seeds

Anderson, James D.; Moore, Thomas C.
Plant Physiology , Volume 42 (11) – Nov 1, 1967
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References (30)

Publisher
Oxford University Press
Copyright
Copyright © 2021 American Society of Plant Biologists
ISSN
0032-0889
eISSN
1532-2548
DOI
10.1104/pp.42.11.1527
Publisher site
See Article on Publisher Site

Abstract

Abstract Mevalonate-14C was incorporated into (—)-kaurene-14C in cell-free extracts of immature pea (Pisum sativum L.) seeds. The identification of 14C-product as (—)-kaurene was based on: A) comparison with authentic (—)-kaurene on thin-layer and gas-liquid chromatography; and B) oxidation of 14C-product and (—)-kaurene with osmium tetroxide to form the common derivative kaurane-16,17-diol. The enzyme system is heat labile and is dependent upon ATP and Mg2+ or Mn2-, with Mn2+ being a more effective activator than Mg2+. The reaction rate was proportional to enzyme concentration in reaction mixtures containing 0.45 to 1.8 mg protein n/ml, and was linear with time through 120 minutes in standard reaction mixtures. Enzyme preparations from immature seeds of tall and dwarf peas appeared to synthesize (—)-kaurene at the same rate. Synthesis of (—)-kaurene was readily inhibited by Amo-1618. (2-Chloroethyl)-trimethylammonium chloride (CCC) also inhibited (—)-kaurene synthesis; however, approximately 1000-fold higher concentrations of CCC were required to evoke the same percentages of inhibition as Amo-1618. 1 This investigation was supported in part by Grant GB-4613 from the National Science Foundation. This paper is part of a thesis to be presented by James D. Anderson to the Graduate School of Oregon State University in partial fulfillment of the requirements for the Ph.D. degree. This content is only available as a PDF. © 1967 American Society of Plant Biologists This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)

Journal

Plant Physiology – Oxford University Press

Published: Nov 1, 1967

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