Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2
Nagahama, Kazuhiro and Ogawa, Takahira and Fujii, Takao and Tazaki, Masato and Tanase, Sumio and Morino, Yoshimasa and Fukuda, Hideo,, 137, 2281-2286 (1991),
doi = https://doi.org/10.1099/00221287-137-10-2281,
publicationName = Microbiology Society,
issn = 1350-0872,
abstract= A novel ethylene-forming enzyme that catalyses the formation of ethylene from 2-oxoglutarate was purified from a cell-free extract of Pseudomonas syringae pv. phaseolicola PK2. It was purified about 2800-fold with an overall yield of 53% to a single band of protein after SDS-PAGE. The purified enzyme had a specific activity of 660 nmol ethylene min–1 (mg protein)–1. The molecular mass of the enzyme was approximately 36 kDa by gel filtration and 42 kDa by SDS-PAGE. The isoelectric point and optimum pH were 5·9 and ca. 7·0–7·5 respectively. There was no homology between the N-terminal amino acid sequence of the ethylene-forming enzyme of Ps. syringae pv. phaseolicola PK2 and the sequence of the ethylene-forming enzyme of the fungus Penicillium digitatum IFO 9372. However, the two enzymes have the following properties in common. The presence of 2-oxoglutarate, l-arginine, Fe2+ and oxygen is essential for the enzymic reaction. The enzymes are highly specific for 2-oxoglutarate as substrate and l-arginine as cofactor. EDTA, Tiron, DTNB [5,5′-dithio-bis(2-nitrobenzoate)] and hydrogen peroxide are all effective inhibitors.,
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