Amidase 

Amidases, a member of nitrilase superfamily, catalyzes the hydrolysis of an amide, leading to the formation of carboxylic acid and ammonia. Amidases contain a conserved stretch of approximately 130 amino acids known as the AS sequence, and play a role in important metabolic processes^[1].

9012-56-0

Liquid

Colorless to light yellow

[Amidase]

3.5.1.4

≥ 200 U/mg protein

One unit is defined as the amount of enzyme that will convert 1.0 μmole of acetamide and hydroxylamine to acetohydroxamate and ammonia per min at pH 7.2 at 37°C

Room temperature in continental US; may vary elsewhere.

Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Weber BW, et al. The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning. J Biol Chem. 2013 Oct 4;288(40):28514-23.

  [2]. Weber BW,et.al. The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning. J Biol Chem. 2013 Oct 4;288(40):28514-23.  [Content Brief]

  [3]. Li W, et al. An Amidase Contributes to Full Virulence of Sclerotinia sclerotiorum. Int J Mol Sci. 2022 Sep 23;23(19):11207.  [Content Brief]