Glycine Oxidase H244K, Bacillus subtilis recombinant | 7845

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 -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.

7845 | Glycine Oxidase H244K Bacillus subtilis recombinant DataSheet

Biomolecule/Target: Glycine Oxidase

Synonyms: Glycine oxidase, glycine oxygen oxidoreductase (deaminating), GO

Alternates names: Apolipoprotein E4, APOE, apolipoprotein, apolipoproteins

Taglines: 90% Pure Active Bacillus subtilis recombinant Glycine Oxidase H244K which shows a higher substrate specificity ratio for glycine versus sarcosine

NCBI Gene ID #:

NCBI Gene Symbol:

Gene Source: Bacillus subtilis

Accession #:

Recombinant: Yes

Source: E. coli

Purity by SDS-PAGEs: 90%

Assay: SDS-PAGE

Purity: N/A

Assay #2: N/A

Endotoxin Level: N/A

Activity (Specifications/test method): 1200 mU/mg

Biological activity: N/A

Results: 1200 mU/mg

Binding Capacity: N/A

Unit Definition: One unit is defined as the amount of enzyme required to convert one micromole of glycine into glyoxylate and hydrogen peroxide at pH 8.5 at 37°C.

Molecular Weight: 34.4 kDa

Concentration: 4.0 mg/ml

Appearance: Liquid

Physical form description: 4.0 mg/ml in 20 mM potassium phosphate, 100 mM NaCl, pH 8.0 and 10% glycerol

Reconstitution Instructions: Reconstitute in dHO to a concentration of 0.1-1.0 mg/ml. The solution can then be diluted into other aqueous buffers and store at 4°C for 1 week or –20°C for future use.

Amino acid sequence: N/A