Skip to Content
Merck
All Photos(1)

Documents

A6691

Sigma-Aldrich

Amidase from Pseudomonas aeruginosa

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

Synonym(s):

Acrylamide Amidohydrolase, Acylase

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
Enzyme Commission number:
MDL number:
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.

storage temp.

−20°C

Gene Information

Pseudomonas aeruginosa PAO1 ... PA4163(880181)

Looking for similar products? Visit Product Comparison Guide

Related Categories

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

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Customers Also Viewed

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)
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
Esterases with an introduced amidase-like hydrogen bond in the transition state have increased amidase specificity.
Per-Olof Syrén et al.
Chembiochem : a European journal of chemical biology, 13(5), 645-648 (2012-03-02)
Arthur J L Cooper et al.
Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology, 163(1), 108-120 (2012-05-23)
Many cancer cells have a strong requirement for glutamine. As an aid for understanding this phenomenon the (18)F-labeled 2S,4R stereoisomer of 4-fluoroglutamine [(2S,4R)4-FGln] was previously developed for in vivo positron emission tomography (PET). In the present work, comparative enzymological studies

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service