Abstract
The ethylene-forming enzyme, which is responsible for the final stage of ethylene synthesis in plants, has been partially purified from melon fruits. The enzyme has a molecular weight of 41 000, a pH optimum at about pH 7.5, an apparent K m of 60 μM, and although it resembles many 2-oxoglutarate-dependent dioxygenases in its requirement for ascorbate and Fe 2+, it does not require 2-oxoglutarate for activity. The enzyme is inhibited by SH-reagents, n-propyl gallate, 1,2-dihydroxynaphthalene, CO 2+, Ni 2+, Cu 2+, Zn 2+ and Mn 2+, but is insensitive to cycloheximide and protonophores.
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