Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2

J Gen Microbiol. 1991 Oct;137(10):2281-6. doi: 10.1099/00221287-137-10-2281.


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.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / antagonists & inhibitors
  • Bacterial Proteins / isolation & purification*
  • Bacterial Proteins / metabolism
  • Enzyme Activation / drug effects
  • Ethylenes / metabolism*
  • Lyases / antagonists & inhibitors
  • Lyases / isolation & purification*
  • Lyases / metabolism
  • Molecular Sequence Data
  • Pseudomonas / enzymology*
  • Species Specificity


  • Bacterial Proteins
  • Ethylenes
  • ethylene
  • Lyases
  • ethylene forming enzyme
  • ethylene-forming enzyme, Pseudomonas