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Literature summary extracted from

  • Powlowski, J.B.; Dagley, S.; Massey, V.; Ballou, D.P.
    Properties of anthranilate hydroxylase (deaminating), a flavoprotein from Trichosporon cutaneum (1987), J. Biol. Chem., 262, 69-74.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.13.35 2-Aminonicotinate activates Cutaneotrichosporon cutaneum
1.14.13.35 N-Formyl anthranilate activates Cutaneotrichosporon cutaneum
1.14.13.35 salicylate activates Cutaneotrichosporon cutaneum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.13.35 50000
-
 2 * 50000, SDS-PAGE Cutaneotrichosporon cutaneum
1.14.13.35 95000
-
 gel filtration Cutaneotrichosporon cutaneum

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.35 Cutaneotrichosporon cutaneum
-
 yeast
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.35 using ammonium sulfate precipitation, column chromatography on DE23-cellulose, phenyl-Sepharose and S-300 Sephacryl Cutaneotrichosporon cutaneum

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.35 anthranilate + NADPH + H+ + O2 = 2,3-dihydroxybenzoate + NADP+ + NH3 mechanism proposed involving imine formation and hydrolysis during the reaction with the flavin peroxide formed from reduced enzyme flavin and molecular oxygen Cutaneotrichosporon cutaneum
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.13.35 4.4
-
-
 Cutaneotrichosporon cutaneum

Storage Stability

EC Number Storage Stability Organism
1.14.13.35 -20°C, in the dark, Na+/K+ phosphate buffer, pH 7.4, 0.1 mM EDTA, stable for at least 6 months Cutaneotrichosporon cutaneum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.35 2-hydrazinebenzoate + NADH + O2
-
 Cutaneotrichosporon cutaneum ?
-
 ?
1.14.13.35 3-hydroxyanthranilate + NADPH + O2
-
 Cutaneotrichosporon cutaneum ?
-
 ?
1.14.13.35 3-methylanthranilate + NADPH + O2
-
 Cutaneotrichosporon cutaneum ? + NADP+ + NH3
-
 ?
1.14.13.35 anthranilate + NADPH + O2
-
 Cutaneotrichosporon cutaneum 2,3-dihydroxybenzoate + NADP+ + NH3 2,3-dihydroxybenzoate i.e. o-pyrocatechuate, oxygen atom at the 3-position of the product 2,3-dihydroxybenzoate originates from O2, that at the 2-position is derived from H2O ?
1.14.13.35 N,N-dimethylanthranilate + NADPH + O2
-
 Cutaneotrichosporon cutaneum ?
-
 ?
1.14.13.35 N-methylanthranilate + NADPH + O2
-
 Cutaneotrichosporon cutaneum 2,3-dihydroxybenzoate + NADP+ + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.13.35 dimer 2 * 50000, SDS-PAGE Cutaneotrichosporon cutaneum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.35 25
-
 assay at Cutaneotrichosporon cutaneum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.35 7.7
-
-
 Cutaneotrichosporon cutaneum

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.14.13.35 5.5 9.8 less than 1% of maximal activity at pH 5.5 and pH 9.8 Cutaneotrichosporon cutaneum

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.14.13.35 5.9 9.1 4°C, stable for at least 3 days Cutaneotrichosporon cutaneum

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.35 FAD flavoprotein Cutaneotrichosporon cutaneum
1.14.13.35 FAD 2 mol FAD per mol enzyme Cutaneotrichosporon cutaneum
1.14.13.35 NADPH
-
 Cutaneotrichosporon cutaneum