The Enzyme Database

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Accepted name: 2-oxoglutarate dioxygenase (ethene-forming)
Reaction: 2-oxoglutarate + O2 = ethene + 3 CO2 + H2O
Glossary: ethene = ethylene
Other name(s): ethylene-forming enzyme; EFE; 2-oxoglutarate dioxygenase (ethylene-forming); 2-oxoglutarate:oxygen oxidoreductase (decarboxylating, ethylene-forming)
Systematic name: 2-oxoglutarate:oxygen oxidoreductase (decarboxylating, ethene-forming)
Comments: This is one of two simultaneous reactions catalysed by the enzyme, which is responsible for ethene production in bacteria of the Pseudomonas syringae group. In the other reaction [EC, 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)] the enzyme catalyses the mono-oxygenation of both 2-oxoglutarate and L-arginine, forming succinate, carbon dioxide and 5-hydroxy-L-arginine, which is subsequently cleaved into guanidine and (S)-1-pyrroline-5-carboxylate.The enzymes catalyse two cycles of the ethene-forming reaction for each cycle of the succinate-forming reaction, so that the stoichiometry of the products ethene and succinate is 2:1.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Nagahama, K., Ogawa, T., Fujii, T., Tazaki, M., Tanase, S., Morino, Y. and Fukuda, H. Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2. J. Gen. Microbiol. 137 (1991) 2281–2286. [DOI] [PMID: 1770346]
2.  Fukuda, H., Ogawa, T., Tazaki, M., Nagahama, K., Fujii, T., Tanase, S. and Morino, Y. Two reactions are simultaneously catalyzed by a single enzyme: the arginine-dependent simultaneous formation of two products, ethylene and succinate, from 2-oxoglutarate by an enzyme from Pseudomonas syringae. Biochem. Biophys. Res. Commun. 188 (1992) 483–489. [DOI] [PMID: 1445291]
3.  Fukuda, H., Ogawa, T., Ishihara, K., Fujii, T., Nagahama, K., Omata, T., Inoue, Y., Tanase, S. and Morino, Y. Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2. Biochem. Biophys. Res. Commun. 188 (1992) 826–832. [DOI] [PMID: 1445325]
[EC created 2011]

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