אסיף מאגר המחקר החקלאי

Purification and characterization of S-linalool synthase, an enzyme involved in the production of floral scent in Clarkia breweri

Year:

1995

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Volume :

316

Co-Authors:

Pichersky, E., Biology Department, University of Michigan, Ann Arbor, MI 48109, United States
Lewinsohn, E., Biology Department, University of Michigan, Ann Arbor, MI 48109, United States
Croteau, R., Biology Department, University of Michigan, Ann Arbor, MI 48109, United States

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Abstract:

S-Linalool is one of the volatiles emitted by Clarkia breweri Grey [Green] flowers to attract its moth pollinator. S-Linalool synthase, the enzyme that stereoselectively converts the ubiquitous C10 intermediate GPP to S-linalool, is abundant in stigmata of freshly opened flowers, and it was purified to >95% homogeneity by anion-exchange and hydroxyapatite chromatography. S-Linalool synthase is operationally soluble as are other monoterpene synthases, has a K(m) of 0.9 μM for geranyl pyrophosphate, exhibits a strict requirement for a divalent metal cofactor with a preference for Mn2+ (K(m) = 45 μM), and shows an optimal pH of 7.4. The enzyme is active as a monomer of 76 ± 3 kDa as determined by gel permeation chromatography and polyacrylamide gel electrophoresis. Neither S- nor R-linalyl pyrophosphates are substrates for the C. breweri S-linalool synthase, although this tertiary allylic pyrophosphate ester is a bound intermediate in the biosynthesis of cyclic monoterpenes from geranyl pyrophosphate in many plant species, where it also serves as an alternate substrate.

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