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EC 1.14.15.37 Details

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EC number

1.14.15.37

Accepted name

luteothin monooxygenase

Reaction

luteothin + 2 O₂ + 4 reduced ferredoxin [iron-sulfur] cluster + 4 H⁺ = aureothin + 3 H₂O + 4 oxidized ferredoxin [iron-sulfur] cluster (overall reaction);;(1a) luteothin + O₂ + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H⁺ = (7R)-7-hydroxyluteothin + H₂O + 2 oxidized ferredoxin [iron-sulfur] cluster;;(1b) (7R)-7-hydroxyluteothin + O₂ + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H⁺ = aureothin + 2 H₂O + 2 oxidized ferredoxin [iron-sulfur] cluster

Other name(s)

aurH (gene name)

Systematic name

luteothin,ferredoxin:oxygen oxidoreductase (aureothin-forming)

Comment

The enzyme, characterized from the bacterium Streptomyces thioluteus, is a bifunctional cytochrome P-450 (heme-thiolate) protein that catalyses both the hydroxylation of its substrate and formation of a furan ring, the final step in the biosynthesis of the antibiotic aureothin. In the bacteria Streptomyces orinoci and Streptomyces spectabilis an orthologous enzyme catalyses a similar reaction that forms spectinabilin.

History

created 2019

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

1.4.1 With NAD⁺ or NADP⁺ as acceptor

1.4.2 With a cytochrome as acceptor

1.4.3 With oxygen as acceptor

1.4.4 With a disulfide as acceptor

1.4.5 With a quinone or other compound as acceptor

1.4.7 With an iron-sulfur protein as acceptor

1.4.9 With a copper protein as acceptor

1.4.98. undefined

1.4.99 With unknown physiological acceptors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

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)

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

1.14.1 With NADH or NADPH as one donor (deleted sub-subclass)

1.14.2 With ascorbate as one donor (deleted sub-subclass)

1.14.3 With reduced pteridine as one donor (deleted sub-subclass)

1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor

1.14.12 With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into the other donor

1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor

1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor

1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor

1.14.15.1 camphor 5-monooxygenase

1.14.15.2 camphor 1,2-monooxygenase

1.14.15.3 alkane 1-monooxygenase

1.14.15.4 steroid 11β-monooxygenase

1.14.15.5 corticosterone 18-monooxygenase

1.14.15.6 cholesterol monooxygenase (side-chain-cleaving)

1.14.15.7 choline monooxygenase

1.14.15.8 steroid 15β-monooxygenase

1.14.15.9 spheroidene monooxygenase

1.14.15.10 (+)-camphor 6-endo-hydroxylase

1.14.15.11 pentalenic acid synthase

1.14.15.12 pimeloyl-[acyl-carrier protein] synthase

1.14.15.13 pulcherriminic acid synthase

1.14.15.14 methyl-branched lipid ω-hydroxylase

1.14.15.15 cholestanetriol 26-monooxygenase

1.14.15.16 vitamin D₃ 24-hydroxylase

1.14.15.17 pheophorbide a oxygenase

1.14.15.18 calcidiol 1-monooxygenase

1.14.15.19 C-19 steroid 1α-hydroxylase

1.14.15.20 heme oxygenase (biliverdin-producing, ferredoxin)

1.14.15.21 zeaxanthin epoxidase

1.14.15.22 vitamin D 1,25-hydroxylase

1.14.15.23 chloroacetanilide N-alkylformylase

1.14.15.24 β-carotene 3-hydroxylase

1.14.15.25 p-cymene methyl-monooxygenase

1.14.15.26 toluene methyl-monooxygenase

1.14.15.27 β-dihydromenaquinone-9 ω-hydroxylase

1.14.15.28 cholest-4-en-3-one 26-monooxygenase [(25R)-3-oxocholest-4-en-26-oate forming]

1.14.15.29 cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]

1.14.15.30 3-ketosteroid 9α-monooxygenase

1.14.15.31 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase

1.14.15.32 pentalenene oxygenase

1.14.15.33 pikromycin synthase

1.14.15.34 20-oxo-5-O-mycaminosyltylactone 23-monooxygenase

1.14.15.35 6-deoxyerythronolide B hydroxylase

1.14.15.36 sterol 14α-demethylase (ferredoxin)

1.14.15.37 luteothin monooxygenase

1.14.15.38 N,N-dimethyl phenylurea N-demethylase

1.14.15.39 epi-isozizaene 5-monooxygenase

1.14.16 With reduced pteridine as one donor, and incorporation of one atom of oxygen into the other donor

1.14.17 With reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor

1.14.18 With another compound as one donor, and incorporation of one atom of oxygen into the other donor

1.14.19 With oxidation of a pair of donors resulting in the reduction of O₂ to two molecules of water

1.14.20 With 2-oxoglutarate as one donor, and the other dehydrogenated

1.14.21 With NADH or NADPH as one donor, and the other dehydrogenated

1.14.99 Miscellaneous

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

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.97.1 Sole sub-subclass for oxidoreductases that do not belong in the other subclasses

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)