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Native Arthrobacter sp. Tyramine Oxidase

Cat No.
DIA-158
Description
Amine oxidases (AO) are enzymes that catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containing (EC 1.4.3.4) and copper-containing (EC 1.4.3.6). Copper-containing AO act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor: RCH2NH2 + H2O + O2 ↔ RCHO + NH3 + H2O2. The 3 substrates of this enzyme are primary amines (RCH2NH2), H2O, and O2, whereas its 3 products are RCHO, NH3, and H2O2.
Abbr
Tyramine Oxidase (Arthrobacter sp.)
Source
Arthrobacter sp.
Applications
Useful for enzymatic determiantion of leucine aminopeptidase
Appearance
White to light brown powder
Product Overview
Native Tyramine Oxidase (EC 1.4.3.4) was purified from Arthrobacter sp..
Form
Freeze dried powder
Enzyme Commission Number
EC 1.4.3.6
Activity
> 3 U/mg
CAS No.
9001-53-0
pH Stability
6.0-8.0 (37°C, 60 mins)
Optimum pH
7
Thermal stability
Stable at 45°C and below (pH 7.5, 5 mins)
Storage
Store in tightly closed containers, desiccated, protected from light, at-20°C.
Synonyms
Tyramine Oxidase; TOD; EC 1.4.3.6
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Realted Protocols
PLASMA-AMINE-OXIDASE -Enzymatic Assay Protocol
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