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EC 1.13.11.60 Details

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EC number

1.13.11.60

Accepted name

linoleate 8R-lipoxygenase

Reaction

linoleate + O₂ = (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate

Other name(s)

linoleic acid 8R-dioxygenase, 5,8-LDS (bifunctional enzyme), 7,8-LDS (bifunctional enzyme), 5,8-linoleate diol synthase (bifunctional enzyme), 7,8-linoleate diol synthase (bifunctional enzyme), PpoA

Systematic name

linoleate:oxygen (8R)-oxidoreductase

Comment

The enzyme contains heme [1,4]. The bifunctional enzyme from Aspergillus nidulans uses different heme domains to catalyse two separate reactions. Linoleic acid is oxidized within the N-terminal heme peroxidase domain to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, which is subsequently isomerized by the C-terminal P-450 heme thiolate domain to (5S,8R,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.5, 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase) [1]. The bifunctional enzyme from Gaeumannomyces graminis also catalyses the oxidation of linoleic acid to (8R,9Z,12Z)-8-hydroperoxyoctadeca-9,12-dienoate, but its second domain isomerizes it to (7S,8S,9Z,12Z)-5,8-dihydroxyoctadeca-9,12-dienoate (cf. EC 5.4.4.6, 9,12-octadecadienoate 8-hydroperoxide 8S-isomerase) [4].

History

created 2011

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.6.1 With NAD⁺ or NADP⁺ as acceptor

1.6.2 With a heme protein as acceptor

1.6.2.1 created 1961, deleted 1965

1.6.2.2 cytochrome-b₅ reductase

1.6.2.3 created 1972, deleted 1965

1.6.2.4 NADPH—hemoprotein reductase

1.6.2.5 NADPH—cytochrome-c₂ reductase

1.6.2.6 leghemoglobin reductase

1.6.3 With oxygen as acceptor

1.6.4 With a disulfide as acceptor (deleted sub-subclass)

1.6.5 With a quinone or similar compound as acceptor

1.6.6 With a nitrogenous group as acceptor

1.6.7 With an iron-sulfur protein as acceptor (deleted sub-subclass)

1.6.8 With a flavin as acceptor (deleted sub-subclass)

1.6.99 With unknown physiological acceptors

1.7 Acting on other nitrogenous compounds as donors

1.8 Acting on a sulfur group of donors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.13.1. undefined

1.13.11 With incorporation of two atoms of oxygen

1.13.11.1 catechol 1,2-dioxygenase

1.13.11.2 catechol 2,3-dioxygenase

1.13.11.3 protocatechuate 3,4-dioxygenase

1.13.11.4 gentisate 1,2-dioxygenase

1.13.11.5 homogentisate 1,2-dioxygenase

1.13.11.6 3-hydroxyanthranilate 3,4-dioxygenase

1.13.11.7 created 1965 as EC 1.13.1.7, transferred 1972 to EC 1.13.11.7, deleted 1980

1.13.11.8 protocatechuate 4,5-dioxygenase

1.13.11.9 2,5-dihydroxypyridine 5,6-dioxygenase

1.13.11.10 7,8-dihydroxykynurenate 8,8a-dioxygenase

1.13.11.11 tryptophan 2,3-dioxygenase

1.13.11.12 linoleate 13S-lipoxygenase

1.13.11.13 ascorbate 2,3-dioxygenase

1.13.11.14 2,3-dihydroxybenzoate 3,4-dioxygenase

1.13.11.15 3,4-dihydroxyphenylacetate 2,3-dioxygenase

1.13.11.16 3-carboxyethylcatechol 2,3-dioxygenase

1.13.11.17 indole 2,3-dioxygenase

1.13.11.18 persulfide dioxygenase

1.13.11.19 cysteamine dioxygenase

1.13.11.20 cysteine dioxygenase

1.13.11.21 created 1972, deleted 2001

1.13.11.22 caffeate 3,4-dioxygenase

1.13.11.23 2,3-dihydroxyindole 2,3-dioxygenase

1.13.11.24 quercetin 2,3-dioxygenase

1.13.11.25 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione 4,5-dioxygenase

1.13.11.26 peptide-tryptophan 2,3-dioxygenase

1.13.11.27 4-hydroxyphenylpyruvate dioxygenase

1.13.11.28 2,3-dihydroxybenzoate 2,3-dioxygenase

1.13.11.29 stizolobate synthase

1.13.11.30 stizolobinate synthase

1.13.11.31 arachidonate 12-lipoxygenase

1.13.11.32 2-nitropropane dioxygenase

1.13.11.33 arachidonate 15-lipoxygenase

1.13.11.34 arachidonate 5-lipoxygenase

1.13.11.35 pyrogallol 1,2-oxygenase

1.13.11.36 chloridazon-catechol dioxygenase

1.13.11.37 hydroxyquinol 1,2-dioxygenase

1.13.11.38 1-hydroxy-2-naphthoate 1,2-dioxygenase

1.13.11.39 biphenyl-2,3-diol 1,2-dioxygenase

1.13.11.40 arachidonate 8-lipoxygenase

1.13.11.41 2,4′-dihydroxyacetophenone dioxygenase

1.13.11.42 indoleamine-pyrrole 2,3-dioxygenase

1.13.11.43 lignostilbene αβ-dioxygenase

1.13.11.44 linoleate diol synthase

1.13.11.45 linoleate 11-lipoxygenase

1.13.11.46 4-hydroxymandelate synthase

1.13.11.47 3-hydroxy-4-oxoquinoline 2,4-dioxygenase

1.13.11.48 3-hydroxy-2-methylquinolin-4-one 2,4-dioxygenase

1.13.11.49 chlorite O₂-lyase

1.13.11.50 acetylacetone-cleaving enzyme

1.13.11.51 9-cis-epoxycarotenoid dioxygenase

1.13.11.52 indoleamine 2,3-dioxygenase

1.13.11.53 acireductone dioxygenase (Ni²⁺-requiring)

1.13.11.54 acireductone dioxygenase [iron(II)-requiring]

1.13.11.55 sulfur oxygenase/reductase

1.13.11.56 1,2-dihydroxynaphthalene dioxygenase

1.13.11.57 gallate dioxygenase

1.13.11.58 linoleate 9S-lipoxygenase

1.13.11.59 torulene dioxygenase

1.13.11.60 linoleate 8R-lipoxygenase

1.13.11.61 linolenate 9R-lipoxygenase

1.13.11.62 linoleate 10R-lipoxygenase

1.13.11.63 β-carotene 15,15′-dioxygenase

1.13.11.64 5-nitrosalicylate dioxygenase

1.13.11.65 carotenoid isomerooxygenase

1.13.11.66 hydroquinone 1,2-dioxygenase

1.13.11.67 8′-apo-β-carotenoid 14′,13′-cleaving dioxygenase

1.13.11.68 9-cis-β-carotene 9′,10′-cleaving dioxygenase

1.13.11.69 carlactone synthase

1.13.11.70 all-trans-10′-apo-β-carotenal 13,14-cleaving dioxygenase

1.13.11.71 carotenoid-9′,10′-cleaving dioxygenase

1.13.11.72 2-hydroxyethylphosphonate dioxygenase

1.13.11.73 methylphosphonate synthase

1.13.11.74 2-aminophenol 1,6-dioxygenase

1.13.11.75 all-trans-8′-apo-β-carotenal 15,15′-oxygenase

1.13.11.76 2-amino-5-chlorophenol 1,6-dioxygenase

1.13.11.77 oleate 10S-lipoxygenase

1.13.11.78 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming)

1.13.11.79 aerobic 5,6-dimethylbenzimidazole synthase

1.13.11.80 (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase

1.13.11.81 7,8-dihydroneopterin oxygenase

1.13.11.82 8′-apo-carotenoid 13,14-cleaving dioxygenase

1.13.11.83 4-hydroxy-3-prenylphenylpyruvate oxygenase

1.13.11.84 crocetin dialdehyde synthase

1.13.11.85 exo-cleaving rubber dioxygenase

1.13.11.86 5-aminosalicylate 1,2-dioxygenase

1.13.11.87 endo-cleaving rubber dioxygenase

1.13.11.88 isoeugenol monooxygenase

1.13.11.89 (hydroxymethyl)phosphonate dioxygenase

1.13.11.90 [1-hydroxy-2-(trimethylamino)ethyl]phosphonate dioxygenase (glycine-betaine-forming)

1.13.11.91 3-mercaptopropionate dioxygenase

1.13.11.92 fatty acid α-dioxygenase

1.13.11.93 2-oxoadipate dioxygenase/decarboxylase

1.13.12 With incorporation of one atom of oxygen (internal monooxygenases or internal mixed-function oxidases)

1.13.99 Miscellaneous

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

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Release 2023.1 (January 2023)