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Glycine Oxidase H244K, Bacillus subtilis recombinant protein
Glycine oxidase, glycine oxygen oxidoreductase (deaminating), GO
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O31616 |
|---|---|
| Concentration | 4 |
| Calculated MW | 43.1 kDa (1-369 aa, NT His Tag) |
| Gene ID | 939377 |
|---|---|
| Gene Symbol | thiO |
| Other Names | Glycine oxidase, glycine oxygen oxidoreductase (deaminating), GO |
| Gene Source | Bacillus subtilis |
| Source | E. coli |
| Assay&Purity | SDS-PAGE; ≥90% |
| Assay2&Purity2 | N/A; |
| Recombinant | Yes |
| Results | 1200 mU/mg |
| Sequence | 1-369 aa |
| Target/Specificity | Glycine Oxidase |
| Format | Liquid |
| Storage | -20°C; 4.0 mg/ml in 20 mM potassium phosphate, 100 mM NaCl, pH 8.0 and 10% glycerol |
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Provided below are standard protocols that you may find useful for product applications.
Background
Glycine oxidase (GO) from Bacillus subtilis (EC 1.4.3.19) is a homotetrameric flavin-dependent oxidoreductase. Each GO monomer is non-covalently bound to flavin adenine dinucleotide. GO catalyzes oxidative deamination of various primary and secondary amines (e.g. glycine, sarcosine, N-ethylglycine) and some D-amino acids (e.g. D -alanine, D -proline, D -valine) to the corresponding α-keto acids and hydrogen peroxide. Primarily, glycine oxidase catalyzes the oxidation of glycine in the biosynthesis of thiamine. The variant H244K shows a higher substrate specificity ratio for glycine versus sarcosine and a 5-fold improved specific activity in comparison to the wild-type.
References
Kunst F.,et al.Nature 390:249-256(1997).
Nishiya Y.,et al.FEBS Lett. 438:263-266(1998).
Job V.,et al.J. Biol. Chem. 277:6985-6993(2002).
Settembre E.C.,et al.Biochemistry 42:2971-2981(2003).
Moertl M.,et al.J. Biol. Chem. 279:29718-29727(2004).
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