Enzymatische Aktivierung von Auxinen und ihre Konjugierung mit Glycin

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Abstract
Octanoate-thiokinase, an enzyme from liver mitochondria, was found to catalyze the formation of auxin-coenzyme A esters with several different auxins in the presence of adenosinetriphosphate and coenzyme A (CoA). Evidence was provided to show that indole/acetyl-adenosinemonophosphate was an intermediate in the formation of indoleacetyl-CoA. This intermediate was supplied to the enzyme as the synthetic anhydride, and could lead either to the formation of indoleacetyl-CoA when supplied with CoA or to the formation of indoleacetic acid plus adenosinetriphosphate when supplied with pyrophosphate. Indoleacetyl-CoA was shown to be the intermediary product in the enzymatic formation of indoleacetyl-glycine. 2,4-Dichlorphenoxyacetic acid and [alpha]-naphthylacetic acid were not measurably conjugated with glycine under the same conditions. The results are discussed as to their implication in auxin metabolism in plants.