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Literature summary extracted from

  • Pedotti, M.; Ghisla, S.; Motteran, L.; Molla, G.; Pollegioni, L.
    Catalytic and redox properties of glycine oxidase from Bacillus subtilis (2009), Biochimie, 91, 604-612.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.19 0.15
-
O2 pH 9.0, 25°C Bacillus subtilis
1.4.3.19 0.15
-
O2 pH 6.5, 25°C Bacillus subtilis
1.4.3.19 0.25
-
O2 pH 7.5, 25°C Bacillus subtilis
1.4.3.19 0.28
-
O2 pH 8.5, 25°C Bacillus subtilis
1.4.3.19 0.4
-
O2 pH 9.5, 25°C Bacillus subtilis
1.4.3.19 0.45
-
O2 pH 7.0, 25°C Bacillus subtilis
1.4.3.19 3.8
-
glycine pH 8.5, 25°C Bacillus subtilis
1.4.3.19 5.4
-
glycine pH 7.5, 25°C Bacillus subtilis
1.4.3.19 5.4
-
glycine pH 9.0, 25°C Bacillus subtilis
1.4.3.19 5.6
-
glycine pH 7.0, 25°C Bacillus subtilis
1.4.3.19 9.2
-
glycine pH 6.5, 25°C Bacillus subtilis
1.4.3.19 14.7
-
glycine pH 9.5, 25°C Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.19 Bacillus subtilis O31616
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.3.19 glycine + H2O + O2
-
Bacillus subtilis glyoxylate + NH3 + H2O2 free glycine oxidase forms the anionic red semiquinone upon photoreduction.This species is thermodynamically stable, as indicated by the large separation of the two single-electron reduction potentials of DeltaE 290 mV. The first potential is pH-independent, while the second is dependent. The midpoint reduction potential exhibits a 23.4 mV/pH unit slope, which is consistent with an overall two-electrons/one-proton transfer in the reduction to yield anionic reduced flavin. In the presence of glycolate and at pH 7.5 the potential for the semiquinone-reduced enzyme couple is shifted positively by about 160 mV, this favors a two-electron transfer compared to the free enzyme. Binding of glycolate and sulfite is also affected by pH ?
1.4.3.19 sarcosine + H2O + O2
-
Bacillus subtilis glyoxylate + methylamine + H2O2
-
?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.3.19 0.9
-
glycine pH 6.5, 25°C Bacillus subtilis
1.4.3.19 2.4
-
glycine pH 7.0, 25°C Bacillus subtilis
1.4.3.19 3
-
glycine pH 9.5, 25°C Bacillus subtilis
1.4.3.19 3.6
-
glycine pH 8.0, 25°C Bacillus subtilis
1.4.3.19 4
-
glycine pH 8.5, 25°C Bacillus subtilis
1.4.3.19 4.1
-
glycine pH 9.0, 25°C Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.19 9 10
-
Bacillus subtilis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.4.3.19 6.5 10 the tetrameric oligomeric state of the holoenzyme is not affected within this range Bacillus subtilis
1.4.3.19 7 8 optimal range for stability Bacillus subtilis