2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)

2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming) (EC 1.14.11.34, ethylene-forming enzyme, EFE) is an enzyme with systematic name L-arginine,2-oxoglutarate:oxygen oxidoreductase (succinate-forming).[1][2][3] This enzyme catalyses the following chemical reaction

2-oxoglutarate + L-arginine + O2 succinate + CO2 + guanidine + (S)-1-pyrroline-5-carboxylate + H2O (overall reaction)
(1a) 2-oxoglutarate + L-arginine + O2 succinate + CO2 + L-hydroxyarginine
(1b) L-hydroxyarginine guanidine + (S)-1-pyrroline-5-carboxylate + H2O
2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)
Identifiers
EC no.1.14.11.34
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

2-oxoglutarate/L-arginine monooxygenase/decarboxylase catalyses two cycles of the ethylene-forming reaction.

References

  1. Nagahama K, Ogawa T, Fujii T, Tazaki M, Tanase S, Morino Y, Fukuda H (October 1991). "Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2". Journal of General Microbiology. 137 (10): 2281–6. doi:10.1099/00221287-137-10-2281. PMID 1770346.
  2. Fukuda H, Ogawa T, Tazaki M, Nagahama K, Fujii T, Tanase S, Morino Y (October 1992). "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". Biochemical and Biophysical Research Communications. 188 (2): 483–9. doi:10.1016/0006-291X(92)91081-Z. PMID 1445291.
  3. Fukuda H, Ogawa T, Ishihara K, Fujii T, Nagahama K, Omata T, Inoue Y, Tanase S, Morino Y (October 1992). "Molecular cloning in Escherichia coli, expression, and nucleotide sequence of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. phaseolicola PK2". Biochemical and Biophysical Research Communications. 188 (2): 826–32. doi:10.1016/0006-291X(92)91131-9. PMID 1445325.
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