44187
Amidase
recombinant, expressed in E. coli, ≥1.5 U/mg
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About This Item
CAS Number:
UNSPSC Code:
12352204
EC Number:
232-736-5
MDL number:
recombinant
expressed in E. coli
form
crystal lumps, lumps, powder
specific activity
≥1.5 U/mg
storage temp.
2-8°C
Application
Amidase is used to study metabolic pathways such as the urea cycle, phenylalanine metabolism, tryptophan metabolism, cyanoamino acid metabolism, and styrene degradation. They are used to hydrolyse peptidoglycan substrates and are used in biocatalysis for the chemoselective, regioselective, or enantioselective hydrolysis of various amides. Amidases may be used for the production of antibiotics, the hydrolysis of C-terminal amide groups in peptides, the analysis of glycoproteins, or for the transformation of cyclic imides.
Biochem/physiol Actions
An amidase is a hydrolase that catalyzes the hydrolysis of an amide. Amidase converts a monocarboxylic acid amide and H2O into a monocarboxylate and NH3. Amidases contain a conserved stretch of approximately 130 amino acids which is known as the AS sequence. Amidases possess a highly conserved Ser-Ser-Lys catalytic triad which is responsible for amide hydrolysis.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Other Notes
1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol nicotinamide to nicotinic acid per minute at pH 7.2 and 30°C
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class
13 - Non Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Sandra Trott et al.
Applied and environmental microbiology, 68(7), 3279-3286 (2002-06-29)
The gene for an enantioselective amidase was cloned from Rhodococcus erythropolis MP50, which utilizes various aromatic nitriles via a nitrile hydratase/amidase system as nitrogen sources. The gene encoded a protein of 525 amino acids which corresponded to a protein with
Anna Liza B Valiña et al.
Biochemistry, 43(50), 15657-15672 (2004-12-15)
Peptide amidase (Pam), a hydrolytic enzyme that belongs to the amidase signature (AS) family, selectively catalyzes the hydrolysis of the C-terminal amide bond (CO-NH(2)) of peptides. The recent availability of the X-ray structures of Pam, fatty acid amide hydrolase, and
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)
Trudy-Ann Tucker et al.
Journal of industrial microbiology & biotechnology, 39(11), 1577-1585 (2012-07-31)
Rhodococcus is an important industrial microorganism that possesses diverse metabolic capabilities; it also has a cell envelope, composed of an outer layer of mycolic acids and glycolipids. Selected Rhodococcus species when induced are capable of transforming nitriles to the corresponding
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
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