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EC 1.14.99.67 Details

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EC number

1.14.99.67

Accepted name

α-N-dichloroacetyl-p-aminophenylserinol N-oxygenase

Reaction

α-N-dichloroacetyl-p-aminophenylserinol + reduced acceptor + 2 O₂ = chloramphenicol + acceptor + 2 H₂O

Other name(s)

cmlI (gene name)

Systematic name

α-N-dichloroacetyl-p-aminophenylserinol,acceptor:oxygen oxidoreductase (N-hydroxylating)

Comment

The enzyme, isolated from the bacterium Streptomyces venezuelae, is involved in the biosynthesis of the antibiotic chloramphenicol. It contains a carboxylate-bridged binuclear non-heme iron cluster. The components of the native electron chain have not been identified, although the immediate donor is likely to be an iron-sulfur protein. The reaction mechanism involves formation of an extremely stable peroxo intermediate that catalyses three individual two-electron oxidations via a hydroxylamine and a nitroso intermediates without releasing the intermediates. cf. EC 1.14.99.68, 4-aminobenzoate N-oxygenase.

History

created 2020

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

1.7 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

1.12.1 With NAD⁺ or NADP⁺ as acceptor

1.12.2 With a cytochrome as acceptor

1.12.5 With a quinone or similar compound as acceptor

1.12.7 With an iron-sulfur protein as acceptor

1.12.98 With other, known, physiological acceptors

1.12.99 With unknown physiological acceptors

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

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.17.1 With NAD⁺ or NADP⁺ as acceptor

1.17.2 With a cytochrome as acceptor

1.17.3 With oxygen as acceptor

1.17.4 With a disulfide as acceptor

1.17.5 With a quinone or similar compound as acceptor

1.17.7 With an iron-sulfur protein as acceptor

1.17.8 With a flavin as acceptor

1.17.9 With a copper protein as acceptor

1.17.98 With other, known, physiological acceptors

1.17.99 With unknown physiological acceptors

1.17.99.1 4-methylphenol dehydrogenase (hydroxylating)

1.17.99.2 ethylbenzene hydroxylase

1.17.99.3 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA 24-hydroxylase

1.17.99.4 uracil/thymine dehydrogenase

1.17.99.5 bile-acid 7α-dehydroxylase

1.17.99.6 epoxyqueuosine reductase

1.17.99.7 formate dehydrogenase (acceptor)

1.17.99.8 limonene dehydrogenase

1.17.99.9 heme a synthase

1.17.99.10 steroid C-25 hydroxylase

1.17.99.11 3-oxo-Δ¹-steroid hydratase/dehydrogenase

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

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)