EC 1.14.20.7 - 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)

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IntEnz Enzyme Nomenclature
EC 1.14.20.7

Names

Accepted name:
2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)
Other names:
ethylene-forming enzyme
EFE
ethene-forming enzyme
Systematic name:
L-arginine,2-oxoglutarate:oxygen oxidoreductase (succinate-forming)

Reactions

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Nagahama, K., Ogawa, T., Fujii, T., Tazaki, M., Tanase, S., Morino, Y., Fukuda, H.
    Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2.
    J. Gen. Microbiol. 137 : 2281-2286 (1991). [PMID: 1770346]
  2. 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.
    Biochem. Biophys. Res. Commun. 188 : 483-489 (1992). [PMID: 1445291]
  3. Fukuda, H., Ogawa, T., Ishihara, K., Fujii, T., Nagahama, K., Omata, T., Inoue, Y., Tanase, S., 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 : 826-832 (1992). [PMID: 1445325]
  4. Martinez, S., Fellner, M., Herr, C. Q., Ritchie, A., Hu, J., 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 : 11980-11988 (2017). [PMID: 28780854]

[EC 1.14.20.7 created 2011 as EC 1.14.11.34, transferred 2018 to EC 1.14.20.7]