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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)

Sinonimo/i:

Acrylamide Amidohydrolase, Acylase

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About This Item

Numero CAS:
9012-56-0
Classificazione EC (Enzyme Commission):
3.5.1.4 (BRENDA, IUBMB)
Numero MDL:
MFCD00166319
Codice UNSPSC:
12352204
NACRES:
NA.54

Ricombinante

expressed in E. coli

Forma fisica

buffered aqueous glycerol solution

hydroxamate transferase activity

≥200 units/mg protein (biuret)

Concentrazione

14 mg/mL

N° accesso UniProt

Q9HWL8

Temperatura di conservazione

−20°C

Informazioni sul gene

Pseudomonas aeruginosa PAO1 ... PA4163(880181)

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Applicazioni

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 .

Azioni biochim/fisiol

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 .

Definizione di unità

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

Stato fisico

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

Pittogrammi

Health hazard
GHS08

Avvertenze

Danger

Indicazioni di pericolo

H334

Consigli di prudenza

P261 - P284 - P501

Classi di pericolo

Resp. Sens. 1

Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

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

Certificati d'analisi (COA)

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Lisostafina free of DNA contaminants, suitable for Microbiome research, lyophilized powder, ≥500 units/mg protein

Sigma-Aldrich

SAE0091

Lisostafina

Substrate interaction with recombinant amidase from Pseudomonas aeruginosa during biocatalysis
Pacheco R, Karmali A
Biocatalysis and Biotransformation, 27(5/6), 367-376 (2009)
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)
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
Susanne Berendt et al.
Journal of bacteriology, 194(19), 5218-5227 (2012-07-24)
Filamentous cyanobacteria of the order Nostocales display typical properties of multicellular organisms. In response to nitrogen starvation, some vegetative cells differentiate into heterocysts, where fixation of N(2) takes place. Heterocysts provide a micro-oxic compartment to protect nitrogenase from the oxygen
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