Jump to content

2-oxoglutarate dioxygenase (ethylene-forming)

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Dcirovic (talk | contribs) at 01:55, 16 May 2016 (→‎top: clean up using AWB). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

2-oxoglutarate dioxygenase (ethylene-forming)
Identifiers
EC no.1.13.12.19
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

2-oxoglutarate dioxygenase (ethylene-forming) (EC 1.13.12.19, ethylene-forming enzyme, EFE) is an enzyme with systematic name 2-oxoglutarate:oxygen oxidoreductase (decarboxylating, ethylene-forming).[1][2][3] This enzyme catalyses the following chemical reaction

2-oxoglutarate + O2 ethylene + 3 CO2 + H2O

2-oxoglutarate dioxygenase produces ethylene in bacteria of the Pseudomonas syringae group.

References

  1. ^ Nagahama, K.; Ogawa, T.; Fujii, T.; Tazaki, M.; Tanase, S.; Morino, Y.; Fukuda, H. (1991). "Purification and properties of an ethylene-forming enzyme from Pseudomonas syringae pv. phaseolicola PK2". J. Gen. Microbiol. 137 (10): 2281–2286. doi:10.1099/00221287-137-10-2281. PMID 1770346.
  2. ^ Fukuda, H.; Ogawa, T.; Tazaki, M.; Nagahama, K.; Fujii, T.; Tanase, S.; Morino, Y. (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". Biochem. Biophys. Res. Commun. 188: 483–489. 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. (1992). "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. doi:10.1016/0006-291X(92)91131-9. PMID 1445325.

External links