f Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2
- Authors: Kazuhiro Nagahama, Takahira Ogawa, Takao Fujii, Masato Tazaki, Sumio Tanase, Yoshimasa Morino, Hideo Fukuda
- Microbiology, October 1991 137: 2281-2286, doi: 10.1099/00221287-137-10-2281
- Subject: Biochemistry
- Published Online:
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.
© Society for General Microbiology 1991 | Published by the Society for General Microbiology
Full text loading...
Author and Article Information
Figure data loading....