Products

Enzymes for Research, Diagnostic and Industrial Use

Products
Online Inquiry

Our Products Cannot Be Used As Medicines Directly For Personal Use.

24 hour
Promise

Welcome! For price inquiries, please feel free to contact us through the form on the left side. We will get back to you as soon as possible.

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

"Tyramine Oxidase" Total Products Page

Our Products Cannot Be Used As Medicines Directly For Personal Use.

0
Click unfold / close
Inquiry Basket
Delete selected Quote Check Out
Decide to move out of the shopping cart?
Sure No, Back

Please choose product!

< Go Back
You have already added to buy this product