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A6691 Sigma-Aldrich

Amidase from Pseudomonas aeruginosa

recombinant, expressed in E. coli, buffered aqueous glycerol solution, hydroxamate transferase ≥200 units/mg protein (biuret)

Synonym: Acrylamide Amidohydrolase, Acylase

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Properties

Related Categories 3.5.x.x Acting on C-N other than peptides, 3.x.x.x Hydrolases, Biochemicals and Reagents, Cell Biology, Enzyme Class Index,
Quality Level   200
recombinant   expressed in E. coli
form   buffered aqueous glycerol solution
hydroxamate transferase activity   ≥200 units/mg protein (biuret)
concentration   14 mg/mL
storage temp.   −20°C
Gene Information   Pseudomonas aeruginosa PAO1 ... PA4163(880181)

Description

Application

Amidase from Pseudomonas aeruginosa has been used for testing its capability to hydrolyze ochratoxin A.

The importance of these hydrolases in biotechnology is growing rapidly, because their potential applications span through chemical and pharmaceutical industries as well as in bioremediation. Immobilized amidase can be used efficiently for production of acrylic acid from acrylamide, thus converting a toxic ambient contaminant into widely used industrial raw material. Amidases are potential treatments for human immunodeficiency virus and malaria. They may be used to eliminate metal ions in wastewater .

Biochem/physiol Actions

The amidase from Pseudomonas aeruginosa isa 6 × 38-kDa enzyme that catalyzes the hydrolysis of a small range of short aliphatic amides. Each amidase monomer is formed by a globular four-layer αββα sandwich domain with an additional 81-residue long C-terminal segment .

Unit Definition

One unit will convert 1.0 μmole of acetamide and hydroxylamine to acetohydroxamate and ammonia per min at pH 7.2 at 37 °C.

Physical form

Solution in 50% glycerol containing 7 mM 2-mercaptoethanol and phosphate buffer salt

Safety & Documentation

Safety Information

Hazard statements 
Precautionary statements 
RIDADR 
NONH for all modes of transport
WGK Germany 
WGK 2

Documents

Certificate of Analysis (COA)

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Certificate of Origin (COO)

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Protocols & Articles

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Peer-Reviewed Papers
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