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Title: Interactions of methionine and selenomethionine with methionine adenosyltransferase and ethylene-generating systems

Abstract

Since selenomethionine appears to be a better precursor of ethylene in senescing flower tissue of Ipomoea tricolor and in indole acetic acid-treated pea stem sections than is methionine, we compared the effectiveness of selenomethionine and methionine to participate in reactions which may be connected to ethylene biosynthesis. Evidence is presented that selenomethionine is also a better substrate of methionine adenosyltransferase (ATP: methionine S-adenosyltransferase, EC 2.5.1.6) from I. tricolor, the V/sub max/ for selenomethionine being twice as high as that for methionine. The affinity of the enzyme is higher for methionine than for selenomethionine, however. Methionine added to flower tissue together with selenomethionine inhibits the enhancement of ethylene synthesis by the seleno analog. Likewise, methionine reduces the high, selenomethionine-dependent reaction rates of methionine adenosyltransferase from I. tricolor flower tissue. On the other hand, selenomethionine is less effective as an ethylene precursor than is methionine in model systems involving oxidation by free radicals. It was concluded that activation of methionine by methionine adenosyltransferase and formation of S-adenosylmethionine are more likely to be involved in ethylene biosynthesis than is oxidation of methionine by free radicals.

Authors:
;
Publication Date:
Research Org.:
Michigan State Univ., East Lansing
OSTI Identifier:
5578923
DOE Contract Number:  
EY-76-C-02-1338
Resource Type:
Journal Article
Journal Name:
Plant Physiol.; (United States)
Additional Journal Information:
Journal Volume: 63:3
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; ETHYLENE; BIOSYNTHESIS; TRANSFERASES; ENZYME ACTIVITY; ATP; BIOLOGICAL PATHWAYS; METHIONINE; OXIDATION; PLANTS; PRECURSOR; SELENIUM; SUBSTRATES; ALKENES; AMINO ACIDS; CARBOXYLIC ACIDS; CHEMICAL REACTIONS; ELEMENTS; ENZYMES; HYDROCARBONS; LIPOTROPIC FACTORS; NUCLEOTIDES; ORGANIC ACIDS; ORGANIC COMPOUNDS; ORGANIC SULFUR COMPOUNDS; SEMIMETALS; SYNTHESIS; 550200* - Biochemistry; 551000 - Physiological Systems

Citation Formats

Konze, J R, and Kende, H. Interactions of methionine and selenomethionine with methionine adenosyltransferase and ethylene-generating systems. United States: N. p., 1979. Web. doi:10.1104/pp.63.3.507.
Konze, J R, & Kende, H. Interactions of methionine and selenomethionine with methionine adenosyltransferase and ethylene-generating systems. United States. https://doi.org/10.1104/pp.63.3.507
Konze, J R, and Kende, H. Thu . "Interactions of methionine and selenomethionine with methionine adenosyltransferase and ethylene-generating systems". United States. https://doi.org/10.1104/pp.63.3.507.
@article{osti_5578923,
title = {Interactions of methionine and selenomethionine with methionine adenosyltransferase and ethylene-generating systems},
author = {Konze, J R and Kende, H},
abstractNote = {Since selenomethionine appears to be a better precursor of ethylene in senescing flower tissue of Ipomoea tricolor and in indole acetic acid-treated pea stem sections than is methionine, we compared the effectiveness of selenomethionine and methionine to participate in reactions which may be connected to ethylene biosynthesis. Evidence is presented that selenomethionine is also a better substrate of methionine adenosyltransferase (ATP: methionine S-adenosyltransferase, EC 2.5.1.6) from I. tricolor, the V/sub max/ for selenomethionine being twice as high as that for methionine. The affinity of the enzyme is higher for methionine than for selenomethionine, however. Methionine added to flower tissue together with selenomethionine inhibits the enhancement of ethylene synthesis by the seleno analog. Likewise, methionine reduces the high, selenomethionine-dependent reaction rates of methionine adenosyltransferase from I. tricolor flower tissue. On the other hand, selenomethionine is less effective as an ethylene precursor than is methionine in model systems involving oxidation by free radicals. It was concluded that activation of methionine by methionine adenosyltransferase and formation of S-adenosylmethionine are more likely to be involved in ethylene biosynthesis than is oxidation of methionine by free radicals.},
doi = {10.1104/pp.63.3.507},
url = {https://www.osti.gov/biblio/5578923}, journal = {Plant Physiol.; (United States)},
number = ,
volume = 63:3,
place = {United States},
year = {1979},
month = {3}
}