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EC 1.14.11.39 Details

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EC number

1.14.11.39

Accepted name

L-asparagine hydroxylase

Reaction

L-asparagine + 2-oxoglutarate + O₂ = (2S,3S)-3-hydroxyasparagine + succinate + CO₂

Other name(s)

L-asparagine 3-hydroxylase, AsnO

Systematic name

L-asparagine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)

Comment

Requires Fe²⁺. The enzyme is only able to hydroxylate free L-asparagine. It is not active toward D-asparagine. The β-hydroxylated asparagine produced is incorporated at position 9 of the calcium-dependent antibiotic (CDA), an 11-residue non-ribosomally synthesized acidic lipopeptide lactone.

History

created 2013

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

1.6.3 With oxygen as acceptor

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

1.6.4.1 created 1961, deleted 2002

1.6.4.2 created 1961, modified 1989, deleted 2002

1.6.4.3 created 1961, modified 1976, deleted 1983

1.6.4.4 created 1965, deleted 2002

1.6.4.5 created 1972, deleted 2002

1.6.4.6 created 1972, deleted 2002

1.6.4.7 created 1978, deleted 2002

1.6.4.8 created 1989, deleted 2002

1.6.4.9 created 1992, deleted 2002

1.6.4.10 created 1992, deleted 2002

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)

1.14 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

1.14.11.1 γ-butyrobetaine dioxygenase

1.14.11.2 procollagen-proline 4-dioxygenase

1.14.11.3 pyrimidine-deoxynucleoside 2′-dioxygenase

1.14.11.4 procollagen-lysine 5-dioxygenase

1.14.11.5 created 1972, deleted 1976

1.14.11.6 thymine dioxygenase

1.14.11.7 procollagen-proline 3-dioxygenase

1.14.11.8 trimethyllysine dioxygenase

1.14.11.9 flavanone 3-dioxygenase

1.14.11.10 pyrimidine-deoxynucleoside 1′-dioxygenase

1.14.11.11 hyoscyamine (6S)-dioxygenase

1.14.11.12 gibberellin-44 dioxygenase

1.14.11.13 gibberellin 2β-dioxygenase

1.14.11.14 6β-hydroxyhyoscyamine epoxidase

1.14.11.15 gibberellin 3β-dioxygenase

1.14.11.16 peptide-aspartate β-dioxygenase

1.14.11.17 taurine dioxygenase

1.14.11.18 phytanoyl-CoA dioxygenase

1.14.11.19 anthocyanidin synthase

1.14.11.20 deacetoxyvindoline 4-hydroxylase

1.14.11.21 clavaminate synthase

1.14.11.22 flavone synthase

1.14.11.23 flavonol synthase

1.14.11.24 2′-deoxymugineic-acid 2′-dioxygenase

1.14.11.25 mugineic-acid 3-dioxygenase

1.14.11.26 deacetoxycephalosporin-C hydroxylase

1.14.11.27 [histone H3]-dimethyl-L-lysine³⁶ demethylase

1.14.11.28 proline 3-hydroxylase

1.14.11.29 hypoxia-inducible factor-proline dioxygenase

1.14.11.30 hypoxia-inducible factor-asparagine dioxygenase

1.14.11.31 thebaine 6-O-demethylase

1.14.11.32 codeine 3-O-demethylase

1.14.11.33 DNA oxidative demethylase

1.14.11.34 2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming)

1.14.11.35 1-deoxypentalenic acid 11β-hydroxylase

1.14.11.36 pentalenolactone F synthase

1.14.11.37 kanamycin B dioxygenase

1.14.11.38 verruculogen synthase

1.14.11.39 L-asparagine hydroxylase

1.14.11.40 enduracididine β-hydroxylase

1.14.11.41 L-arginine hydroxylase

1.14.11.42 tRNA^Phe (7-(3-amino-3-carboxypropyl)wyosine³⁷-C²)-hydroxylase

1.14.11.43 (S)-dichlorprop dioxygenase (2-oxoglutarate)

1.14.11.44 (R)-dichlorprop dioxygenase (2-oxoglutarate)

1.14.11.45 L-isoleucine 4-hydroxylase

1.14.11.46 2-aminoethylphosphonate dioxygenase

1.14.11.47 [50S ribosomal protein L16]-arginine 3-hydroxylase

1.14.11.48 xanthine dioxygenase

1.14.11.49 uridine-5′-phosphate dioxygenase

1.14.11.50 (–)-deoxypodophyllotoxin synthase

1.14.11.51 DNA N⁶-methyladenine demethylase

1.14.11.52 validamycin A dioxygenase

1.14.11.53 mRNA N⁶-methyladenine demethylase

1.14.11.54 mRNA N¹-methyladenine demethylase

1.14.11.55 ectoine hydroxylase

1.14.11.56 L-proline cis-4-hydroxylase

1.14.11.57 L-proline trans-4-hydroxylase

1.14.11.58 ornithine lipid ester-linked acyl 2-hydroxylase

1.14.11.59 2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase

1.14.11.60 scopoletin 8-hydroxylase

1.14.11.61 feruloyl-CoA 6-hydroxylase

1.14.11.62 trans-4-coumaroyl-CoA 2-hydroxylase

1.14.11.63 peptidyl-lysine (3S)-dioxygenase

1.14.11.64 glutarate dioxygenase

1.14.11.65 [histone H3]-dimethyl-L-lysine⁹ demethylase

1.14.11.66 [histone H3]-trimethyl-L-lysine⁹ demethylase

1.14.11.67 [histone H3]-trimethyl-L-lysine⁴ demethylase

1.14.11.68 [histone H3]-trimethyl-L-lysine²⁷ demethylase

1.14.11.69 [histone H3]-trimethyl-L-lysine³⁶ demethylase

1.14.11.70 7-deoxycylindrospermopsin hydroxylase

1.14.11.71 methylphosphonate hydroxylase

1.14.11.72 [2-(trimethylamino)ethyl]phosphonate dioxygenase

1.14.11.73 [protein]-arginine 3-hydroxylase

1.14.11.74 L-isoleucine 3¹-dioxygenase

1.14.11.75 3¹-hydroxy-L-isoleucine 4-dioxygenase

1.14.11.76 L-glutamate 3(R)-hydroxylase

1.14.11.77 alkyl sulfatase

1.14.11.78 (R)-3-[(carboxymethyl)amino]fatty acid dioxygenase/decarboxylase

1.14.11.79 protein-L-histidine (3S)-3-hydroxylase

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

1.15 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

1.97.1 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)