Misplaced Pages

Linolenate 9R-lipoxygenase

Article snapshot taken from Wikipedia with creative commons attribution-sharealike license. Give it a read and then ask your questions in the chat. We can research this topic together.
Linolenate 9R-lipoxygenase
Identifiers
EC no.1.13.11.61
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

Linolenate 9R-lipoxygenase (EC 1.13.11.61, NspLOX, (9R)-LOX, linoleate 9R-dioxygenase) is an enzyme with systematic name alpha-linolenate:oxygen (9R)-oxidoreductase. This enzyme catalyses the following chemical reaction

alpha-linolenate + O2 {\displaystyle \rightleftharpoons } (9R,10E,12Z,15Z)-9-hydroperoxyoctadeca-10,12,15-trienoate

In cyanobacteria the enzyme is involved in oxylipin biosynthesis.

References

  1. Jernerén F, Hoffmann I, Oliw EH (March 2010). "Linoleate 9R-dioxygenase and allene oxide synthase activities of Aspergillus terreus". Archives of Biochemistry and Biophysics. 495 (1): 67–73. doi:10.1016/j.abb.2009.12.022. PMID 20043865.
  2. Andreou AZ, Vanko M, Bezakova L, Feussner I (June 2008). "Properties of a mini 9R-lipoxygenase from Nostoc sp. PCC 7120 and its mutant forms". Phytochemistry. 69 (9): 1832–7. doi:10.1016/j.phytochem.2008.03.002. PMID 18439634.
  3. Lang I, Göbel C, Porzel A, Heilmann I, Feussner I (March 2008). "A lipoxygenase with linoleate diol synthase activity from Nostoc sp. PCC 7120" (PDF). The Biochemical Journal. 410 (2): 347–57. doi:10.1042/BJ20071277. PMID 18031288.

External links

Oxidoreductases: monooxygenases (EC 1.13)
1.13.11: two atoms of oxygen
1.13.12: one atom of oxygen
1.13.99: other
Enzymes
Activity
Regulation
Classification
Kinetics
Types
Portal: Category: