| Autor: |
John Kamsteeg, Jan van Brederode, Gerrit van Nigtevecht, Paul M. Verschuren |
| Rok vydání: |
1981 |
| Předmět: |
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| Zdroj: |
Zeitschrift für Pflanzenphysiologie. 102:435-442 |
| ISSN: |
0044-328X |
| DOI: |
10.1016/s0044-328x(81)80178-x |
| Popis: |
Summary An enzyme catalyzing the hydroxylation of the 3-position of p -coumaroyl-Coenzyme A has been demonstrated in petal extracts of Silene dioica plants. For optimal activity NADPH, FAD, and molecular oxygen are necessary. The hydroxlating activity is governed by gene P ; in pink petals of p/p plants this activity was absent. In vivo gene P controls both the hydroxylation pattern of the anthocyanin B-ring and that of the acyl group. The enzyme can use p -coumaric acid as non-substrate effector. In this case hydrogen peroxide is formed and p -coumaric acid remains unchanged during the course of the reaction. Although the enzyme isolated from petals of p/p plants was not able to hydroxylate p -coumaroyl- CoA, it could still use p -coumaric acid as non-substrate effector. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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