Skip Navigation

This Article
Right arrow Full Text
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 ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (10)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Yamamoto, K.-i.
Right arrow Articles by Komamine, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yamamoto, K.-i.
Right arrow Articles by Komamine, A.
Agricola
Right arrow Articles by Yamamoto, K.-i.
Right arrow Articles by Komamine, A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 2001, Vol. 42, No. 9 969-975
© 2001 Oxford University Press

Isolation and Purification of Tyrosine Hydroxylase from Callus Cultures of Portulaca grandiflora

Ken-ichi Yamamoto1, Naoko Kobayashi1, Kunijiro Yoshitama2, Susumu Teramoto2,4 and Atsushi Komamine3

1 Graduate School of Science and Technology, Kumamoto University, Kurokami 2-39-1, Kumamoto, 860-8555 Japan 2 Department of Biological Science, Faculty of Science, Kumamoto University, Kurokami 2-39-1, Kumamoto, 860-8555 Japan 3 The Research Institute of Evolutionary Biology, Kamiyoga 2-4-28, Setagaya-ku, Tokyo, 158-0098 Japan

Tyrosine hydroxylase was separated from polyphenol oxidase activity and was highly purified from betacyanin producing callus cultures of Portulaca grandiflora. The purified enzyme catalyzed the formation of DOPA (L-3,4-dihydroxyphenylalanine) from tyrosine and required the pterin compounds (6-methyl-5,6,7,8-tetrahydropterin; 5,6,7,8-tetrahydrobiopterin; 6,7-dimethyl-5,6,7,8-tetrahydropterin) as coenzyme. The Km values for tyrosine and 6-methyl-5,6,7,8-tetrahydropterin were 0.5 mM and 0.15 mM, respectively. This enzyme was activated by Fe2+ and Mn2+, and inhibited by metal chelating agents.

4 Corresponding author: E-mail, dopa@aster.sci.kumamoto-u.ac.jp; Fax, +81-96-356-3714.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Plant Physiol.Home page
A. Noiriel, V. Naponelli, J. F. Gregory III, and A. D. Hanson
Pterin and Folate Salvage. Plants and Escherichia coli Lack Capacity to Reduce Oxidized Pterins
Plant Physiology, March 1, 2007; 143(3): 1101 - 1109.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
G. Sepulveda-Jimenez, P. Rueda-Benitez, H. Porta, and M. Rocha-Sosa
A red beet (Beta vulgaris) UDP-glucosyltransferase gene induced by wounding, bacterial infiltration and oxidative stress
J. Exp. Bot., February 1, 2005; 56(412): 605 - 611.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
A. Goyer, V. Illarionova, S. Roje, M. Fischer, A. Bacher, and A. D. Hanson
Folate Biosynthesis in Higher Plants. cDNA Cloning, Heterologous Expression, and Characterization of Dihydroneopterin Aldolases
Plant Physiology, May 1, 2004; 135(1): 103 - 111.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
L. Christinet, F. X. Burdet, M. Zaiko, U. Hinz, and J.-P. Zryd
Characterization and Functional Identification of a Novel Plant 4,5-Extradiol Dioxygenase Involved in Betalain Pigment Biosynthesis in Portulaca grandiflora
Plant Physiology, January 1, 2004; 134(1): 265 - 274.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.