S7897
Sarcosine Oxidase from Bacillus sp.
lyophilized powder, 25-50 units/mg solid
Sinónimos:
Sarcosine: oxygen oxidoreductase (demethylating)
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About This Item
Productos recomendados
form
lyophilized powder
Quality Level
specific activity
25-50 units/mg solid
mol wt
44 kDa
storage temp.
−20°C
General description
Monomeric sarcosine oxidase (MSOX) is a flavoenzyme that catalyzes the oxidative demethylation of sarcosine (N-methylglycine) to yield glycine, formaldehyde, and hydrogen peroxide. Monomeric sarcosine oxidase can oxidize other secondary amino acids such as N-methyl-L-alanine, N-ethylglycine, and L-proline.
Sarcosine oxidase is a 44 kDa protein with covalently bound 1 mol of flavin adenine dinucleotide (FAD). It belongs to the family of amino acid oxidases with bound FAD.
Application
Sarcosine oxidase from Bacillus sp. has been used as a positive control for detection of proteins with covalently bound flavin adenine dinucleotide (FAD) by UV. It has also been used in co-immobilization with other enzymes on platinum electrode for preparation of creatinine biosensor.
Sarcosine oxidase has been used in a study as part of a multienzyme cascade, that when immobilized constructed amperometric biosensors. Sarcosine oxidase has also been used in a study to investigate oxidation of amines by flavoproteins.
Unit Definition
One unit will form 1.0 μmole of formaldehyde from sarcosine per min at pH 8.3 at 37 °C.
Physical form
No stabilizers added
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Analytical biochemistry, 421(1), 256-261 (2011-11-10)
Amperometric biosensors based on gold planar or nanocomposite electrode containing multiwalled carbon nanotubes for determination of glycerol were developed. The biosensors were constructed by immobilization of a novel multienzyme cascade consisting of glycerol kinase/creatine kinase/creatinase/sarcosine oxidase/peroxidase between a chitosan "sandwich."
Archives of biochemistry and biophysics, 493(1), 13-25 (2009-08-05)
Many flavoproteins catalyze the oxidation of primary and secondary amines, with the transfer of a hydride equivalent from a carbon-nitrogen bond to the flavin cofactor. Most of these amine oxidases can be classified into two structural families, the D-amino acid
Optimization of the production of Chondrus crispus hexose oxidase in Pichia pastoris
Protein Expression and Purification, 22(2), 189-199 (2001)
Handbook of Flavoproteins: Oxidases, Dehydrogenases and Related Systems, 196-196 (2012)
Journal of biochemistry, 141(6), 799-815 (2007-03-31)
Heterotetrameric sarcosine oxidase from Corynebacterium sp.U-96(SO-U96) contains non-covalent and covalent flavins. Lys-358 and Lys-171 in the beta subunit is present at non-covalent flavin adenine dinucleotide (FAD)- and covalent flavin monodinucleotide (FMN)-binding sites, respectively. The Lys-358 mutant, K358R showed 0.07% activity
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