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EC 1.14.18.2 Details

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EC number

1.14.18.2

Accepted name

CMP-N-acetylneuraminate monooxygenase

Reaction

CMP-N-acetylneuraminate + 2 ferrocytochrome b₅ + O₂ + 2 H⁺ = CMP-N-glycoloylneuraminate + 2 ferricytochrome b₅ + H₂O

Other name(s)

CMP-N-acetylneuraminic acid hydroxylase, CMP-Neu5Ac hydroxylase, cytidine monophosphoacetylneuraminate monooxygenase, N-acetylneuraminic monooxygenase, cytidine-5′-monophosphate-N-acetylneuraminic acid hydroxylase

Systematic name

CMP-N-acetylneuraminate,ferrocytochrome-b₅:oxygen oxidoreductase (N-acetyl-hydroxylating)

CAS registry number

116036-67-0

Comment

This enzyme contains both a Rieske-type [2Fe-2S] cluster and a second iron site. The ferricytochrome b₅ produced is reduced by NADH and cytochrome-b₅ reductase (EC 1.6.2.2). The enzyme can be activated by Fe²⁺ or Fe³⁺.

History

created 1992 as EC 1.14.13.45, transferred 2003 to EC 1.14.18.2

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

1.13 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

1.14.16 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

1.14.99.1 prostaglandin-endoperoxide synthase

1.14.99.2 kynurenine 7,8-hydroxylase

1.14.99.3 heme oxygenase (biliverdin-producing)

1.14.99.4 progesterone monooxygenase

1.14.99.5 created 1972, modified 1986, modified 2000, deleted 2000

1.14.99.6 created 1972, modified 2000, deleted 2000

1.14.99.7 squalene monooxygenase

1.14.99.8 created 1972, deleted 1984

1.14.99.9 steroid 17α-monooxygenase

1.14.99.10 steroid 21-monooxygenase

1.14.99.11 estradiol 6β-monooxygenase

1.14.99.12 androst-4-ene-3,17-dione monooxygenase

1.14.99.13 created 1972, deleted 1984

1.14.99.14 progesterone 11α-monooxygenase

1.14.99.15 4-methoxybenzoate monooxygenase (O-demethylating)

1.14.99.16 created 1972, deleted 2002

1.14.99.17 created 1972, deleted 1976

1.14.99.18 created 1976, modified 1999, deleted 2003

1.14.99.19 plasmanylethanolamine desaturase

1.14.99.20 phylloquinone monooxygenase (2,3-epoxidizing)

1.14.99.21 Latia-luciferin monooxygenase (demethylating)

1.14.99.22 ecdysone 20-monooxygenase

1.14.99.23 3-hydroxybenzoate 2-monooxygenase

1.14.99.24 steroid 9α-monooxygenase

1.14.99.25 created 1986, deleted 2000

1.14.99.26 2-hydroxypyridine 5-monooxygenase

1.14.99.27 juglone 3-monooxygenase

1.14.99.28 linalool 8-monooxygenase

1.14.99.29 deoxyhypusine monooxygenase

1.14.99.30 carotene 7,8-desaturase

1.14.99.31 myristoyl-CoA 11-(E) desaturase

1.14.99.32 myristoyl-CoA 11-(Z) desaturase

1.14.99.33 Δ¹²-fatty acid dehydrogenase

1.14.99.34 monoprenyl isoflavone epoxidase

1.14.99.35 thiophene-2-carbonyl-CoA monooxygenase

1.14.99.36 β-carotene 15,15′-monooxygenase

1.14.99.37 taxadiene 5α-hydroxylase

1.14.99.38 cholesterol 25-monooxygenase

1.14.99.39 ammonia monooxygenase

1.14.99.40 5,6-dimethylbenzimidazole synthase

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

1.14.99.42 zeaxanthin 7,8-dioxygenase

1.14.99.43 β-amyrin 24-hydroxylase

1.14.99.44 diapolycopene oxygenase

1.14.99.45 carotene ε-monooxygenase

1.14.99.46 pyrimidine oxygenase

1.14.99.47 (+)-larreatricin hydroxylase

1.14.99.48 heme oxygenase (staphylobilin-producing)

1.14.99.49 2-hydroxy-5-methyl-1-naphthoate 7-hydroxylase

1.14.99.50 γ-glutamyl hercynylcysteine S-oxide synthase

1.14.99.51 hercynylcysteine S-oxide synthase

1.14.99.52 L-cysteinyl-L-histidinylsulfoxide synthase

1.14.99.53 lytic chitin monooxygenase

1.14.99.54 lytic cellulose monooxygenase (C1-hydroxylating)

1.14.99.55 lytic starch monooxygenase

1.14.99.56 lytic cellulose monooxygenase (C4-dehydrogenating)

1.14.99.57 heme oxygenase (mycobilin-producing)

1.14.99.58 heme oxygenase (biliverdin-IX-β and δ-forming)

1.14.99.59 tryptamine 4-monooxygenase

1.14.99.60 3-demethoxyubiquinol 3-hydroxylase

1.14.99.61 cyclooctat-9-en-7-ol 5-monooxygenase

1.14.99.62 cyclooctatin synthase

1.14.99.63 β-carotene 4-ketolase

1.14.99.64 zeaxanthin 4-ketolase

1.14.99.65 4-amino-L-phenylalanyl-[CmlP-peptidyl-carrier-protein] 3-hydroxylase

1.14.99.66 [histone H3]-N⁶,N⁶-dimethyl-L-lysine⁴ FAD-dependent demethylase

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

1.14.99.68 4-aminobenzoate N-oxygenase

1.14.99.69 tRNA 2-(methylsulfanyl)-N⁶-isopentenyladenosine³⁷ hydroxylase

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)

3.1 Acting on ester bonds

3.2 Glycosylases

3.3 Acting on ether bonds

3.4 Acting on peptide bonds (peptidases)

3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

3.6 Acting on acid anhydrides

3.7 Acting on carbon-carbon bonds

3.8 Acting on halide bonds

3.9 Acting on phosphorus-nitrogen bonds

3.10 Acting on sulfur-nitrogen bonds

3.10.1 Acting on sulfur-nitrogen bonds (only sub-subclass identified to date)

3.11 Acting on carbon-phosphorus bonds

3.12 Acting on sulfur-sulfur bonds

3.13 Acting on carbon-sulfur bonds

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Release 2023.1 (January 2023)