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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)

Synonyme(s) :

Acrylamide Amidohydrolase, Acylase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Produit recombinant

expressed in E. coli

Forme

buffered aqueous glycerol solution

hydroxamate transferase activity

≥200 units/mg protein (biuret)

Concentration

14 mg/mL

Numéro d'accès UniProt

Température de stockage

−20°C

Informations sur le gène

Pseudomonas aeruginosa PAO1 ... PA4163(880181)

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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 .

Actions biochimiques/physiologiques

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 .

Définition de l'unité

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

Forme physique

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

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Les clients ont également consulté

Jorge Andrade et al.
The Journal of biological chemistry, 282(27), 19598-19605 (2007-04-20)
Microbial amidases belong to the thiol nitrilases family and have potential biotechnological applications in chemical and pharmaceutical industries as well as in bioremediation. The amidase from Pseudomonas aeruginosa isa6 x 38-kDa enzyme that catalyzes the hydrolysis of a small range
Butyramide-utilizing mutants of Pseudomonas aeruginosa 8602 which produce an amidase with altered substrate specificity.
J E Brown et al.
Journal of general microbiology, 57(2), 273-285 (1969-08-01)
Sebastian Zoll et al.
Journal of bacteriology, 194(15), 3789-3802 (2012-05-23)
The bifunctional major autolysin Atl plays a key role in staphylococcal cell separation. Processing of Atl yields catalytically active amidase (AM) and glucosaminidase (GL) domains that are each fused to repeating units. The two repeats of AM (R1 and R2)
Vikash Babu et al.
Colloids and surfaces. B, Biointerfaces, 89, 277-282 (2011-09-29)
In this study, enzymatic surface modification of polyacrylonitrile was studied using nitrile metabolizing enzyme of Amycolatopsis sp. IITR 215. During enzymatic treatment of polyacrylonitrile at pH of 5.8 and 7, it was observed that the conversion of cyano group to
Peng Chen et al.
Chemical communications (Cambridge, England), 48(29), 3482-3484 (2012-02-11)
Amidase-catalyzed desymmetrization of meso-N-heterocyclic dicarboxamides under very mild conditions provided a highly efficient and practical method for the preparation of enantiomerically pure carbamoyl-substituted heterocyclic amino acids that were unique and versatile platforms for the construction of both antipodes of aza-sugar

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