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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)

Sinónimos:

Acrylamide Amidohydrolase, Acylase

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About This Item

Número de CAS:
9012-56-0
Comisión internacional de enzimas:
3.5.1.4 (BRENDA, IUBMB)
MDL number:
MFCD00166319
UNSPSC Code:
12352204
NACRES:
NA.54

recombinant

expressed in E. coli

form

buffered aqueous glycerol solution

hydroxamate transferase activity

≥200 units/mg protein (biuret)

concentration

14 mg/mL

UniProt accession no.

Q9HWL8

storage temp.

−20°C

Gene Information

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 .

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

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Sigma-Aldrich

SAE0091

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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)
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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
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
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