|
|
|
| Authors: | S. Satoh, T. Yoshioka, Y. Kosugi |
| Keywords: | ACC (1-aminocyclopropane-1-carboxylate) synthase, Carnation flower petals, Dianthus caryophyllus, Ethylene, Mechanism-based inactivation |
Abstract:
We investigated the properties of ACC (1-aminocyclopropane-l-carboxylate) synthase obtained from senescing carnation (Dianthus caryophyllus L.) flower petals.
The enzyme had a pH optimum at 8.5–9.0 and the Km for S-adenosyl-L-methionine was 39.0±8.7 μM. The molecular mass of the enzyme was estimated to be 52 kDa by gel-filtration chromatography, indicating that it was present and active in a monomeric form.
The enzyme was very susceptible to the mechanism-based inactivation (the irreversible inactivation by the substrate during catalytic reaction); the half-life for the inactivation was 11.2±3.7 min.
|
Download Adobe Acrobat Reader (free software to read PDF files) |
|