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Literature summary for 1.4.3.19 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
Search for more literature for 1.4.3.19

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O31616
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
sarcosine + H2O + O2
-
 Bacillus subtilis glyoxylate + methylamine + H2O2
-
 ?

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9 10
-
 Bacillus subtilis

pH Stability

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