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Literature summary extracted from

  • Kido, T.; Soda, K.; Suzuki, T.; Asada, K.
    A new oxygenase, 2-nitropropane dioxygenase of Hansenula mrakii. Enzymologic and spectrophotometric properties (1976), J. Biol. Chem., 251, 6994-7000.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.13.12.16 2,2'-dipyridyl
-
Cyberlindnera mrakii
1.13.12.16 2,4,6-tripyridyl-s-triazine
-
Cyberlindnera mrakii
1.13.12.16 o-phenanthroline
-
Cyberlindnera mrakii

General Stability

EC Number General Stability Organism
1.13.12.16 denaturation by sodium dithionite Cyberlindnera mrakii
1.13.12.16 gradual and irreversible loss of activity after treatment with 1% sodium lauryl sulfate or 6 M guanidine HCl, activity is reduced to 50% of its initial activity after 50 min at 37°C, complete loss of activity after 10 h Cyberlindnera mrakii
1.13.12.16 immediate denaturation with 8 M urea or thiourea Cyberlindnera mrakii

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.12.16 2-mercaptoethanol
-
Cyberlindnera mrakii
1.13.12.16 8-hydroxyquinoline strong inhibition Cyberlindnera mrakii
1.13.12.16 cysteine marked decrease in enzyme activity Cyberlindnera mrakii
1.13.12.16 GSH marked decrease in enzyme activity Cyberlindnera mrakii
1.13.12.16 HgCl2 moderate and potent inhibitor Cyberlindnera mrakii
1.13.12.16 additional information EDTA does not inhibit the enzyme significantly. Iodoacetate is almost ineffective Cyberlindnera mrakii
1.13.12.16 N-ethylmaleimide
-
Cyberlindnera mrakii
1.13.12.16 NaHSO3
-
Cyberlindnera mrakii
1.13.12.16 NEM
-
Cyberlindnera mrakii
1.13.12.16 Nitromethane inhibits noncompetitively Cyberlindnera mrakii
1.13.12.16 p-chloromercuribenzoate
-
Cyberlindnera mrakii
1.13.12.16 PCMB
-
Cyberlindnera mrakii
1.13.12.16 Tiron i.e. pyrocatechol-3,5-disulfonate disodium salt; i.e. pyrocatechol-3,5-disulfonate disodium salt, strong inhibition Cyberlindnera mrakii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.12.16 0.3
-
O2
-
Cyberlindnera mrakii
1.13.12.16 4.2
-
3-Nitro-2-butanol neutral form of substrate Cyberlindnera mrakii
1.13.12.16 6.8
-
nitroethane
-
Cyberlindnera mrakii
1.13.12.16 6.8
-
3-Nitro-2-pentanol
-
Cyberlindnera mrakii
1.13.12.16 21.3
-
2-Nitropropane
-
Cyberlindnera mrakii
1.13.12.16 24.3
-
nitroethane
-
Cyberlindnera mrakii
1.13.12.16 25.6
-
1-Nitropropane
-
Cyberlindnera mrakii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.12.16 Fe3+ contains 1 g atom of non-heme iron per mol of enzyme Cyberlindnera mrakii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.12.16 25000
-
1 * 25000 + 1 * 39000, SDS-PAGE Cyberlindnera mrakii
1.13.12.16 39000
-
1 * 25000 + 1 * 39000, SDS-PAGE Cyberlindnera mrakii
1.13.12.16 60000
-
gel filtration Cyberlindnera mrakii
1.13.12.16 64000
-
equilibrium sedimentation Cyberlindnera mrakii

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.16 Cyberlindnera mrakii
-
-
-
1.13.12.16 Cyberlindnera mrakii
-
IF0 0895
-
1.13.12.16 Cyberlindnera mrakii IF0 0895
-
IF0 0895
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.12.16 to homogeneity Cyberlindnera mrakii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.16 1-nitropropane + O2 23.4% of the activity with 2-nitropropane Cyberlindnera mrakii propionaldehyde + HNO2
-
?
1.13.12.16 1-nitropropane + O2 23.4% of the activity with 2-nitropropane Cyberlindnera mrakii IF0 0895 propionaldehyde + HNO2
-
?
1.13.12.16 2-nitropropane + O2
-
Cyberlindnera mrakii acetone + HNO2
-
?
1.13.12.16 2-nitropropane + O2
-
Cyberlindnera mrakii IF0 0895 acetone + HNO2
-
?
1.13.12.16 3-nitro-2-butanol + O2 13% of the activity with 2-nitropropane Cyberlindnera mrakii 3-hydroxy-butane-2-one + HNO2
-
?
1.13.12.16 3-nitro-2-butanol + O2 slight oxidation Cyberlindnera mrakii 3-hydroxy-butane-2-one + HNO2
-
?
1.13.12.16 3-nitro-2-pentanol + O2 40.6% of the activity with 2-nitropropane Cyberlindnera mrakii 2-hydroxy-pentane-3-one + HNO2
-
?
1.13.12.16 3-nitropropionic acid + O2 11.7% of the activity with 2-nitropropane Cyberlindnera mrakii ?
-
?
1.13.12.16 additional information sodium dithionite also reduces both the enzyme-bound FAD and Fe3+ under anaerobic conditions Cyberlindnera mrakii ?
-
?
1.13.12.16 additional information sodium dithionite also reduces both the enzyme-bound FAD and Fe3+ under anaerobic conditions Cyberlindnera mrakii IF0 0895 ?
-
?
1.13.12.16 nitroethane + O2 88% of the activity with nitroethane Cyberlindnera mrakii acetaldehyde + HNO2
-
?
1.13.12.16 nitroethane + O2 88% of the activity with nitroethane Cyberlindnera mrakii IF0 0895 acetaldehyde + HNO2
-
?
1.13.12.16 nitromethane + O2 no activity Cyberlindnera mrakii formaldehyde + HNO2
-
?
1.13.12.16 nitromethane + O2 is not a substrate, under anaerobic conditions. The aerobic dialysis of the enzyme treated with nitromethane causes reoxidation of only the Fe2+ Cyberlindnera mrakii formaldehyde + HNO2
-
?

Subunits

EC Number Subunits Comment Organism
1.13.12.16 dimer 1 * 25000 + 1 * 39000, SDS-PAGE Cyberlindnera mrakii

Synonyms

EC Number Synonyms Comment Organism
1.13.12.16 2-nitropropane dioxygenase
-
Cyberlindnera mrakii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.12.16 40
-
-
Cyberlindnera mrakii

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.13.12.16 20 45
-
Cyberlindnera mrakii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.12.16 additional information
-
when the enzyme is dialyzed against 10 mM potassium phosphate buffer (pH 7.0) immediately after reduction by dithionite, the absorption spectrum similar to that of the native enzyme appears with concomitant restoration of approximately 80% of the activity Cyberlindnera mrakii
1.13.12.16 8
-
-
Cyberlindnera mrakii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.13.12.16 7 8.5
-
Cyberlindnera mrakii
1.13.12.16 7 8.5 when the enzyme is acidified to pH 3.0 and treated in the same way, the prosthetic groups do not dissociate from the protein and almost full activity remained Cyberlindnera mrakii

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.12.16 FAD contains 0.95 mol of FAD per mol of enzyme Cyberlindnera mrakii
1.13.12.16 FAD contains 0.95 mol of FAD per mol of enzyme. The enzyme-bound FAD is reduced by 2-nitropropane under anaerobic conditions Cyberlindnera mrakii