Format

Send to

Choose Destination
Arch Biochem Biophys. 1995 Feb 1;316(2):803-7.

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

Author information

1
Biology Department, University of Michigan, Ann Arbor 48109.

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 Km of 0.9 microM for geranyl pyrophosphate, exhibits a strict requirement for a divalent metal cofactor with a preference for Mn2+ (Km = 45 microM), 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.

PMID:
7864636
DOI:
10.1006/abbi.1995.1107
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center