KEGG ENZYME: 1.13.11.45

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

[ag:AAK81882]