Radiolabeling of a wound-inducible pyridoxal phosphate-utilizing enzyme: Evidence for its identification as ACC synthase
1-Aminocyclopropane-1-carboxylic acid (ACC) synthase, a pyridoxal phosphate-utilizing enzyme, catalyzes the conversion of S-adenosylmethionine to ACC, the rate-limiting step in the biosynthesis of the plant hormone ethylene. We report the partial purification (400-fold) of ACC synthase from wounded...
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Veröffentlicht in: | Archives of biochemistry and biophysics 1987-03, Vol.253 (2), p.333-340 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | 1-Aminocyclopropane-1-carboxylic acid (ACC) synthase, a pyridoxal phosphate-utilizing enzyme, catalyzes the conversion of
S-adenosylmethionine to ACC, the rate-limiting step in the biosynthesis of the plant hormone ethylene. We report the partial purification (400-fold) of ACC synthase from wounded pink tomato pericarp. Further purification results in a decrease in specific activity apparently due to the instability of the enzyme. Radiolabeling of a pyridoxal phosphate-utilizing protein in the ACC synthase-enriched fraction was achieved by reduction using tritiated sodium borohydride. Evidence that this radiolabeled protein is ACC synthase is presented. |
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ISSN: | 0003-9861 1096-0384 |
DOI: | 10.1016/0003-9861(87)90186-X |