Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

Plant Physiology Preview
Published on February 22, 2005; 10.1104/pp.104.053306

This Article
Right arrow Full Text (Plant Physiology Preview (PDF))
Right arrow All Versions of this Article:
137/3/873    most recent
pp.104.053306v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (18)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Davis, E. M.
Right arrow Articles by Croteau, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Davis, E. M.
Right arrow Articles by Croteau, R.
Agricola
Right arrow Articles by Davis, E. M.
Right arrow Articles by Croteau, R.

Received September 16, 2004
Returned for revision December 17, 2004
Accepted December 20, 2004

Monoterpene Metabolism. Cloning, Expression, and Characterization of Menthone Reductases from Peppermint

Edward M. Davis , Kerry L. Ringer , Marie E. McConkey , and Rodney Croteau *

Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164-6340

* Corresponding author; email: croteau{at}wsu.edu.

(-)-Menthone is the predominant monoterpene produced in the essential oil of maturing peppermint (Mentha x piperita) leaves during the filling of epidermal oil glands. This early biosynthetic process is followed by a second, later oil maturation program (approximately coincident with flower initiation) in which the C3-carbonyl of menthone is reduced to yield (-)-(3R)-menthol and (+)-(3S)-neomenthol by two distinct NADPH-dependent ketoreductases. An activity-based in situ screen, by expression in Escherichia coli of 23 putative redox enzymes from an immature peppermint oil gland expressed sequence tag library, was used to isolate a cDNA encoding the latter menthone:(+)-(3S)-neomenthol reductase. Reverse transcription-PCR amplification and RACE were used to acquire the former menthone:(-)-(3R)-menthol reductase directly from mRNA isolated from the oil gland secretory cells of mature leaves. The deduced amino acid sequences of these two reductases share 73% identity, provide no apparent subcellular targeting information, and predict inclusion in the short-chain dehydrogenase/reductase family of enzymes. The menthone:(+)-(3S)-neomenthol reductase cDNA encodes a 35,722-D protein, and the recombinant enzyme yields 94% (+)-(3S)-neomenthol and 6% (-)-(3R)-menthol from (-)-menthone as substrate, and 86% (+)-(3S)-isomenthol and 14% (+)-(3R)-neoisomenthol from (+)-isomenthone as substrate, has a pH optimum of 9.3, and Km values of 674 µM, > 1 mM, and 10 µM for menthone, isomenthone, and NADPH, respectively, with a kcat of 0.06 s-1. The recombinant menthone:(-)-(3R)-menthol reductase has a deduced size of 34,070 D and converts (-)-menthone to 95% (-)-(3R)-menthol and 5% (+)-(3S)-neomenthol, and (+)-isomenthone to 87% (+)-(3R)-neoisomenthol and 13% (+)-(3S)-isomenthol, displays optimum activity at neutral pH, and has Km values of 3.0 µM, 41 µM, and 0.12 µM for menthone, isomenthone, and NADPH, respectively, with a kcat of 0.6 s-1. The respective activities of these menthone reductases account for all of the menthol isomers found in the essential oil of peppermint. Biotechnological exploitation of these genes could lead to improved production yields of (-)-menthol, the principal and characteristic flavor component of peppermint.




This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
J. Ziegler, W. Brandt, R. Geissler, and P. J. Facchini
Removal of Substrate Inhibition and Increase in Maximal Velocity in the Short Chain Dehydrogenase/Reductase Salutaridine Reductase Involved in Morphine Biosynthesis
J. Biol. Chem., September 25, 2009; 284(39): 26758 - 26767.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
H. W. Choi, B. G. Lee, N. H. Kim, Y. Park, C. W. Lim, H. K. Song, and B. K. Hwang
A Role for a Menthone Reductase in Resistance against Microbial Pathogens in Plants
Plant Physiology, September 1, 2008; 148(1): 383 - 401.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
R. Rios-Estepa, G. W. Turner, J. M. Lee, R. B. Croteau, and B. M. Lange
A systems biology approach identifies the biochemical mechanisms regulating monoterpenoid essential oil composition in peppermint
PNAS, February 26, 2008; 105(8): 2818 - 2823.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
R. Geissler, W. Brandt, and J. Ziegler
Molecular Modeling and Site-Directed Mutagenesis Reveal the Benzylisoquinoline Binding Site of the Short-Chain Dehydrogenase/Reductase Salutaridine Reductase
Plant Physiology, April 1, 2007; 143(4): 1493 - 1503.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
K. L. Ringer, E. M. Davis, and R. Croteau
Monoterpene Metabolism. Cloning, Expression, and Characterization of (-)-Isopiperitenol/(-)-Carveol Dehydrogenase of Peppermint and Spearmint
Plant Physiology, March 1, 2005; 137(3): 863 - 872.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2005 by the American Society of Plant Biologists