Skip Navigation

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 Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Hyodo, H.
Right arrow Articles by Tanaka, K.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Hyodo, H.
Right arrow Articles by Tanaka, K.
Agricola
Right arrow Articles by Hyodo, H.
Right arrow Articles by Tanaka, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 1986, Vol. 27, No. 3 391-398
© 1986

Article

Inhibition of 1-Aminocyclopropane-l-carboxylic Acid Synthase Activity by Polyamines, Their Related Compounds and Metabolites of S-adenosylmethionine

Hiroshi Hyodo and Kuniaki Tanaka

Department of Horticulture, Faculty of Agriculture, Shizuoka University Ohya, Shizuoka 422, Japan

Basic amino acids, monoamines, diamines and polyamines inhibited the activity of 1-aminocyclopropane-1-carboxylic acid (ACC) synthase extracted from wounded mesocarp tissue of winter squash fruit (Cucurbita maxima Duch.). Among the amines tested, polyamines were highly effective, while the synthetic triamine, 1,8-diamino-4-aminomethyloctane, was an even stronger inhibitor than the polyamine spermine. Polyamines inhibited ACC synthase activity in a non-competitive manner, while metabolic inhibitors such as aminoethoxyvinylglycine and aminooxyacetic acid inhibited ACC synthase activity competitively, showing much lower Ki values than those of polyamines. ACC synthase activity was also inhibited by intermediates of the methionine-recycling pathway, 5'-methylthioadenosine and {alpha}-keto-{gamma}-methylthiobutyric acid and by S-adenosylhomocysteine, a product of transmethylation of S-adenosylmethionine.

It appears that polyamines not only inhibit ACC synthase activity but also suppress the induction of the enzyme. However, unlike previous reports, polyamines did not inhibit in vivo ethylene forming enzyme activity in the wounded mesocarp tissue.

(Received October 24, 1985; Accepted January 10, 1986)
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
S.-I. Oh, J. Park, S. Yoon, Y. Kim, S. Park, M. Ryu, M. J. Nam, S. H. Ok, J.-K. Kim, J.-S. Shin, et al.
The Arabidopsis Calcium Sensor Calcineurin B-Like 3 Inhibits the 5'-Methylthioadenosine Nucleosidase in a Calcium-Dependent Manner
Plant Physiology, December 1, 2008; 148(4): 1883 - 1896.
[Abstract] [Full Text] [PDF]

Home page
 J Exp BotHome page
G. Rzewuski, K. A. Cornell, L. Rooney, K. Burstenbinder, M. Wirtz, R. Hell, and M. Sauter
OsMTN encodes a 5'-methylthioadenosine nucleosidase that is up-regulated during submergence-induced ethylene synthesis in rice (Oryza sativa L.)
J. Exp. Bot., April 1, 2007; 58(6): 1505 - 1514.
[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.