KEGG   ENZYME: 1.13.11.45
Entry
EC 1.13.11.45               Enzyme                                 
Name
linoleate 11-lipoxygenase;
linoleate dioxygenase;
manganese lipoxygenase
Class
Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of two atoms of oxygen
Sysname
linoleate:oxygen 11S-oxidoreductase
Reaction(IUBMB)
linoleate + O2 = (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate [RN:R05718]
Reaction(KEGG)
R05718
Substrate
linoleate [CPD:C01595];
O2 [CPD:C00007]
Product
(9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate [CPD:C07338]
Comment
The product (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate, is converted, more slowly, into (9Z,11E)-(13R)-13-hydroperoxyoctadeca-9,11-dienoate. The enzyme from the fungus Gaeumannomyces graminis requires Mn2+. It also acts on alpha-linolenate, whereas gamma-linolenate is a poor substrate. Oleate and arachidonate are not substrates.
History
EC 1.13.11.45 created 2000
Pathway
ec00591  Linoleic acid metabolism
Orthology
K21794  linoleate 11-lipoxygenase
Reference
1  [PMID:9582346]
  Authors
Hamberg M, Su C, Oliw E.
  Title
Manganese lipoxygenase. Discovery of a bis-allylic hydroperoxide as product and intermediate in a lipoxygenase reaction.
  Journal
J Biol Chem 273:13080-8 (1998)
DOI:10.1074/jbc.273.21.13080
Reference
2  [PMID:9778131]
  Authors
Oliw EH, Su C, Skogstrom T, Benthin G.
  Title
Analysis of novel hydroperoxides and other metabolites of oleic, linoleic, and linolenic acids by liquid chromatography-mass spectrometry with ion trap MSn.
  Journal
Lipids 33:843-52 (1998)
DOI:10.1007/s11745-998-0280-0
Reference
3  [PMID:9582345]
  Authors
Su C, Oliw EH
  Title
Manganese lipoxygenase. Purification and characterization.
  Journal
J Biol Chem 273:13072-9 (1998)
DOI:10.1074/jbc.273.21.13072
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 1.13.11.45
IUBMB Enzyme Nomenclature: 1.13.11.45
ExPASy - ENZYME nomenclature database: 1.13.11.45
BRENDA, the Enzyme Database: 1.13.11.45

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