44187
Amidase
recombinant, expressed in E. coli, ≥1.5 U/mg
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About This Item
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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.
Unit Definition
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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class Code
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
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
Raffaella Gandolfi et al.
Bioorganic & medicinal chemistry letters, 22(16), 5283-5287 (2012-07-17)
The chemoenzymatic deacylation of ramoplanin A2 is described for the first time: ramoplanin A2 was Boc-protected and hydrogenated to Boc-protected tetrahydroramoplanin, which was subsequently deacylated using an acylase from Actinoplanes utahensis NRRL 12052. The chemoenzymatic process proceeded with 80% overall
Seemay Chou et al.
Cell reports, 1(6), 656-664 (2012-07-21)
The target range of a bacterial secretion system can be defined by effector substrate specificity or by the efficacy of effector delivery. Here, we report the crystal structure of Tse1, a type VI secretion (T6S) bacteriolytic amidase effector from Pseudomonas
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