Description
Aliases
thiO, goxB, yjbR, BSU11670
Antibody Type
Polyclonal Antibody
Species
Bacillus subtilis
Uniprot ID
O31616
Immunogen
Recombinant Bacillus subtilis Glycine oxidase protein (1-369AA)
Raised In
Rabbit
Species Reactivity
Bacillus subtilis
Tested Applications
ELISA;Not yet tested in other applications.
Background / Function
Catalyzes the FAD-dependent oxidative deamination of various amines and D-amino acids to yield the corresponding alpha-keto acids, ammonia/amine, and hydrogen peroxide. Oxidizes sarcosine (N-methylglycine), N-ethylglycine and glycine. Can also oxidize the herbicide glyphosate (N-phosphonomethylglycine). Displays lower activities on D-alanine, D-valine, D-proline and D-methionine. Does not act on L-amino acids and other D-amino acids. Is essential for thiamine biosynthesis since the oxidation of glycine catalyzed by ThiO generates the glycine imine intermediate (dehydroglycine) required for the biosynthesis of the thiazole ring of thiamine pyrophosphate.
Isotype
IgG
Conjugate
Biotin
Storage Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Form
Liquid
Storage
Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze.
Purity
Caprylic Acid Ammonium Sulfate Precipitation purified
Literature
[1]Glyphosate resistance by engineering the flavoenzyme glycine oxidase. Pedotti M., Rosini E., Molla G., Moschetti T., Savino C., Vallone B., Pollegioni L. J. Biol. Chem. 284:36415-36423(2009). [2]Structure-function correlation in glycine oxidase from Bacillus subtilis. Moertl M., Diederichs K., Welte W., Molla G., Motteran L., Andriolo G., Pilone M.S., Pollegioni L. J. Biol. Chem. 279:29718-29727(2004). [3]Structural and mechanistic studies on ThiO, a glycine oxidase essential for thiamin biosynthesis in Bacillus subtilis. Settembre E.C., Dorrestein P.C., Park J.-H., Augustine A.M., Begley T.P., Ealick S.E. Biochemistry 42:2971-2981(2003).Additional information
| Size | 50μg, 100μg |
|---|
