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Purification and characterization of S-linalool synthase, an enzyme involved in the production of floral scent in Clarkia breweri
Year:
1995
Authors :
Lewinsohn, Efraim
;
.
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
Facilitators :
From page:
803
To page:
807
(
Total pages:
5
)
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.
Note:
Related Files :
biosynthesis
Hydro-Lyases
Monoterpenes
odor
odors
plant
terpenes
unclassified drug
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More details
DOI :
10.1006/abbi.1995.1107
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
28042
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:36
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Scientific Publication
Purification and characterization of S-linalool synthase, an enzyme involved in the production of floral scent in Clarkia breweri
316
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
Purification and characterization of S-linalool synthase, an enzyme involved in the production of floral scent in Clarkia breweri
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.
Scientific Publication
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