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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)

Sinônimo(s):

Acrylamide Amidohydrolase, Acylase

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250 UNITS
R$ 3.469,00
1000 UNITS
R$ 6.595,00

About This Item

Número CAS:
Número da licença da enzima:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

R$ 3.469,00


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recombinante

expressed in E. coli

Formulário

buffered aqueous glycerol solution

hydroxamate transferase activity

≥200 units/mg protein (biuret)

concentração

14 mg/mL

nº de adesão UniProt

temperatura de armazenamento

−20°C

Informações sobre genes

Pseudomonas aeruginosa PAO1 ... PA4163(880181)

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Aplicação

Amidase from Pseudomonas aeruginosa has been used for testing its capability to hydrolyze ochratoxin A.[1]
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 [2].

Ações bioquímicas/fisiológicas

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 [2].

Definição da unidade

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

forma física

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

Pictogramas

Health hazard

Palavra indicadora

Danger

Frases de perigo

Declarações de precaução

Classificações de perigo

Resp. Sens. 1

Código de classe de armazenamento

12 - Non Combustible Liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

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


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

Sigma-Aldrich

SAE0091

Lisostafina

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)
Mo-Fei Li et al.
Fish & shellfish immunology, 32(2), 322-330 (2011-12-08)
Peptidoglycan recognition proteins (PGRPs) are a family of innate immune molecules that recognize bacterial peptidoglycan. PGRPs are highly conserved in invertebrates and vertebrates including fish. However, the biological function of teleost PGRP remains largely uninvestigated. In this study, we identified
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)
Ya-Jun Wang et al.
Journal of industrial microbiology & biotechnology, 39(3), 409-417 (2011-09-06)
In this work, a mild, efficient bioconversion of 2,2-dimethylcyclopropanecarbonitrile (DMCPCN) to 2,2-dimethylcyclopropanecarboxamide (DMCPCA) in distilled water system was developed. The isolate FW815 was screened using the enrichment culture technique, displaying strong DMCPCN hydratase activity, and was identified as Rhodococcus boritolerans

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