Reaction: L-arginine + 2-oxoglutarate + O2 = succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O (overall reaction)
(1a) L-arginine + 2-oxoglutarate + O2 = 5-hydroxy-L-arginine + succinate + CO2
(1b) 5-hydroxy-L-arginine = guanidine + L-glutamate-5-semialdehyde
(1c) L-glutamate-5-semialdehyde = (S)-1-pyrroline-5-carboxylate + H2O (spontaneous)
Other name(s): ethene-forming enzyme; ethylene-forming enzyme; EFE
Systematic name: L-arginine,2-oxoglutarate:oxygen oxidoreductase (succinate-forming)
Comments: This is one of two simultaneous reactions catalysed by the enzyme, which is responsible for ethylene production in bacteria of the Pseudomonas syringae group. In the other reaction [EC 1.13.12.19, 2-oxoglutarate dioxygenase (ethene-forming)] the enzyme catalyses the dioxygenation of 2-oxoglutarate forming ethene and three molecules of carbon dioxide.The enzyme catalyses 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, CAS registry number:
References:
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. [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. [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. [PMID: 1445325]
4. Martinez, S., Fellner, M., Herr, C.Q., Ritchie, A., Hu, J. and Hausinger, R.P. Structures and mechanisms of the non-heme Fe(II)- and 2-oxoglutarate-dependent ethylene-forming enzyme: substrate binding creates a twist. J. Am. Chem. Soc. 139 (2017) 11980-11988. [PMID: 28780854]