Plant Physiol. Drug Metab Dispos
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Plant Physiology 98:1364-1371 (1992)
© 1992 American Society of Plant Biologists

This Article
Right arrow Full Text (PDF)
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 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 Google Scholar
Google Scholar
Right arrow Articles by O'Malley, D. M.
Right arrow Articles by Sederoff, R. R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by O'Malley, D. M.
Right arrow Articles by Sederoff, R. R.
Agricola
Right arrow Articles by O'Malley, D. M.
Right arrow Articles by Sederoff, R. R.
Metabolism and Enzymology

Purification, Characterization, and Cloning of Cinnamyl Alcohol Dehydrogenase in Loblolly Pine (Pinus taeda L.) 1

David M. O'Malley, Stephanie Porter and Ronald R. Sederoff

Department of Forestry, North Carolina State University, Raleigh, North Carolina 27695-8008

Cinnamyl alcohol dehydrogenase (CAD, EC 1.1.1. 195) has been purified to homogeneity from differentiating xylem tissue and developing seeds of loblolly pine (Pinus taeda L.). The enzyme is a dimer with a native molecular weight of 82,000 and a subunit molecular weight of 44,000, and is the only form of CAD involved in lignification in differentiating xylem. High levels of loblolly pine CAD enzyme were found in nonlignifying seed tissue. Characterization of the enzyme from both seeds and xylem demonstrated that the enzyme is the same in both tissues. The enzyme has a high affinity for coniferaldehyde (Km = 1.7 micromolar) compared with sinapaldehyde (Km in excess of 100 micromolar). Kinetic data strongly suggest that coniferin is a noncompetitive inhibitor of CAD enzyme activity. Protein sequences were obtained for the N-terminus (28 amino acids) and for two other peptides. Degenerate oligonucleotide primers based on the protein sequences were used to amplify by polymerase chain reaction a 1050 base pair DNA fragment from xylem cDNA. Nucleotide sequence from the cloned DNA fragment coded for the N-terminal protein sequence and an internal peptide of CAD. The N-terminal protein sequence has little similarity with the {lambda}CAD4 clone isolated from bean (MH Walter, J Grima-Pettenati, C Grand, AM Boudet, CJ Lamb [1988] Proc Natl Acad Sci USA 86:5546-5550), which has homology with malic enzyme.

1 This work is supported in part by grants from the U.S. Department of Agriculture (USDA) Competitive Research Grants Program No. 88-37234-4008 and 910-3082, the North Carolina Biotechnology Center, USDA Forest Service Cooperative Agreement No. 29-488, and the North Carolina State University Forest Biotechnology Industrial Associates Group.




This article has been cited by other articles:


Home page
 ScienceHome page
G. A. Tuskan, S. DiFazio, S. Jansson, J. Bohlmann, I. Grigoriev, U. Hellsten, N. Putnam, S. Ralph, S. Rombauts, A. Salamov, et al.
The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).
Science, September 15, 2006; 313(5793): 1596 - 1604.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
M. Cabane, J.-C. Pireaux, E. Leger, E. Weber, P. Dizengremel, B. Pollet, and C. Lapierre
Condensed Lignins Are Synthesized in Poplar Leaves Exposed to Ozone
Plant Physiology, February 1, 2004; 134(2): 586 - 594.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
R. Blanco-Portales, N. Medina-Escobar, J. A. Lopez-Raez, J. A. Gonzalez-Reyes, J. M. Villalba, E. Moyano, J. L. Caballero, and J. Munoz-Blanco
Cloning, expression and immunolocalization pattern of a cinnamyl alcohol dehydrogenase gene from strawberry (Fragariaxananassa cv. Chandler)
J. Exp. Bot., August 1, 2002; 53(375): 1723 - 1734.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. M. Anterola, J.-H. Jeon, L. B. Davin, and N. G. Lewis
Transcriptional Control of Monolignol Biosynthesis in Pinus taeda. FACTORS AFFECTING MONOLIGNOL RATIOS AND CARBON ALLOCATION IN PHENYLPROPANOID METABOLISM
J. Biol. Chem., May 17, 2002; 277(21): 18272 - 18280.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
L. Li, X. F. Cheng, J. Leshkevich, T. Umezawa, S. A. Harding, and V. L. Chiang
The Last Step of Syringyl Monolignol Biosynthesis in Angiosperms Is Regulated by a Novel Gene Encoding Sinapyl Alcohol Dehydrogenase
PLANT CELL, July 1, 2001; 13(7): 1567 - 1586.
[Abstract] [Full Text] [PDF]

Home page
 GeneticsHome page
M. M. Sewell, B. K. Sherman, and D. B. Neale
A Consensus Map for Loblolly Pine (Pinus taeda L.). I. Construction and Integration of Individual Linkage Maps From Two Outbred Three-Generation Pedigrees
Genetics, January 1, 1999; 151(1): 321 - 330.
[Abstract] [Full Text]

Home page
 Proc. Natl. Acad. Sci. USAHome page
I. Allona, M. Quinn, E. Shoop, K. Swope, S. St. Cyr, J. Carlis, J. Riedl, E. Retzel, M. M. Campbell, R. Sederoff, et al.
Analysis of xylem formation in pine by cDNA sequencing
PNAS, August 4, 1998; 95(16): 9693 - 9698.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
J. J. MacKay, D. M. O'Malley, T. Presnell, F. L. Booker, M. M. Campbell, R. W. Whetten, and R. R. Sederoff
Inheritance, gene expression, and lignin characterization in a mutant pine deficient in cinnamyl alcohol dehydrogenase
PNAS, July 22, 1997; 94(15): 8255 - 8260.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1992 by the American Society of Plant Biologists