1.4.3.19: glycine oxidase
This is an abbreviated version!
For detailed information about glycine oxidase, go to the full flat file.
Word Map on EC 1.4.3.19
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1.4.3.19
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d-amino
-
sarcosine
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flavoproteins
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glyphosate
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flavin
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fad
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tryptophylquinone
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flavoenzyme
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herbicide
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d-proline
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homotetrameric
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d-alanine
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pseudoalteromonas
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luteoviolacea
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protein-derived
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thios
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fad-dependent
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site-saturation
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fad-binding
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quinoprotein
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ttq
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half-reaction
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5-enolpyruvylshikimate-3-phosphate
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fad-containing
- 1.4.3.19
-
d-amino
- sarcosine
- flavoproteins
- glyphosate
- flavin
- fad
-
tryptophylquinone
-
flavoenzyme
-
herbicide
- d-proline
-
homotetrameric
- d-alanine
-
pseudoalteromonas
- luteoviolacea
-
protein-derived
-
thios
-
fad-dependent
-
site-saturation
-
fad-binding
-
quinoprotein
- ttq
-
half-reaction
- 5-enolpyruvylshikimate-3-phosphate
-
fad-containing
Reaction
Synonyms
BcGO, glycin oxidase, glycine:oxygen oxidoreductase (deaminating), GlyOX, GO, GOX, GoxA, GOXK, GoxR, LodA, PlGoxA, ThiO
ECTree
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Renatured on EC 1.4.3.19 - glycine oxidase
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the isolated apoprotein species is present in solution as a monomer which rapidly recovers its tertiary structure and converts into the tetrameric holoenzyme following incubation with free FAD. The reconstitution process follows a particular two-stage process, the spectral properties of the reconstituted holoenzyme are virtually indistinguishable from those observed with native glycine oxidase, while the activity is only recovered to about 50%. The urea-induced unfolding process of glycine oxidase can be considered as a two-step process. Only a single transition at 4.5 M urea concentration is observed for the apoprotein form. The chemical denaturation of glycine oxidase holoenzyme is partially reversible