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Literature summary for 1.13.12.19 extracted from

  • Fukuda, H.; Ogawa, T.; Tazaki, M.; Nagahama, K.; Fujii, T.; Tanase, S.; 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 (1992), Biochem. Biophys. Res. Commun., 188, 483-489.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ at the active site, enzyme acts as a bidentate ligand and it forms a complex with Fe2+. The Fe2+ is further coordinated to a tridentate Schiff base of 2-oxoglutarate and L-arginine, whose terminal carboxylate and guanidino groups are trapped by binding sites I and II on the enzyme, respectively Pseudomonas syringae

Organism

Organism UniProt Comment Textmining
Pseudomonas syringae P32021 pv. phaseolicola PK2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoglutarate + O2 presence of oxygen is essential for the ethylene forming reaction by EFE Pseudomonas syringae ethylene + ?
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additional information enzyme catalyzes the formation of ethylene and succinate from 2-oxoglutarate, at a molar ratio of 2:l, reactions of EC 1.13.12.19 and EC 1.14.11.34. In the main reaction, 2-oxoglutarate is dioxygenated to produce one molecule of ethylene and three molecules of carbon dioxide. In the sub-reaction, both 2-oxoglutarate and L-arginine are mono-oxygenated to yield succinate plus carbon dioxide and L-hydroxyarginine, respectively, the latter being further transformed to guanidine and L-delta-pyrroline-5-carboxylate. Dual-circuit mechanism for the entire reaction is proposed, in which the binding of L-arginine and 2-oxoglutarate in a Schiff-base structure generates a common intermediate for two reactions Pseudomonas syringae ?
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Synonyms

Synonyms Comment Organism
EFE
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Pseudomonas syringae
ethylene-forming enzyme
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Pseudomonas syringae