Literature summary for 1.4.3.19 extracted from

Caldinelli, L.; Pedotti, M.; Motteran, L.; Molla, G.; Pollegioni, L.
FAD binding in glycine oxidase from Bacillus subtilis (2009), Biochimie, 91, 1499-1508.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Bacillus subtilis

Protein Variants

Protein Variants	Comment	Organism
A45H/G300C	monomeric in solution. Upon incubation of apoprotein with FAD, neither FAD binding nor enzymatic activity is observed. Slow elimination of urea from partially unfolded mutant in presence of a large excess of FAD and 30% glyccerol does not produce the holoenzyme	Bacillus subtilis
G300C	upon incubation of apoprotein with FAD, neither FAD binding nor enzymatic activity is observed. Slow elimination of urea from partially unfolded mutant in presence of a large excess of FAD and 30% glycerol does not produce the holoenzyme	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	O31616	-	-

Purification (Commentary)

Purification (Comment)	Organism
purification of apoprotein	Bacillus subtilis

Renatured (Commentary)

Renatured (Comment)	Organism
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	Bacillus subtilis

Renatured (Comment)

Organism

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

Bacillus subtilis

Subunits

Subunits	Comment	Organism
More	the isolated apoprotein of glycine oxidase shows high protein fluorescence, high exposure of hydrophobic surfaces, and low temperature stability as compared to the holoenzyme	Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
48	-	melting temperature, apoprotein	Bacillus subtilis
56.9	-	melting temperature, holoenzyme	Bacillus subtilis

Cofactor

Cofactor	Comment	Organism	Structure
FAD	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	Bacillus subtilis