29996
ω-Transaminase
≥0.5 U/mg
recombinant
expressed in E. coli
form
powder
specific activity
≥0.5 U/mg
storage temp.
2-8°C
Biochem/physiol Actions
ω-transaminase catalyzes the removal of the amino group from an amino acid and attaches it to an α-keto acid, producing a new amino acid. Unlike α-transaminase, ω-transaminase shows catalytic activity towards primary amine compounds that do not have a carboxylic group.
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Other Notes
1 U corresponds to the amount of enzyme which converts 1μmol S-α-methylbenzylamine to acetophenone per minute at pH 7.2 and 25°C (in the presence of pyruvate and pyridoxal-5-phosphate)
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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Enzymatic studies on the metabolism of beta-alanine.
O HAYAISHI et al.
The Journal of biological chemistry, 236, 781-790 (1961-03-01)
Lack of stringent stereospecificity in the inactivation of pyridoxal phosphate-dependent enzymes by suicide-substrates.
C Danzin et al.
Progress in clinical and biological research, 144A, 377-385 (1984-01-01)
Hyungdon Yun et al.
Applied and environmental microbiology, 70(4), 2529-2534 (2004-04-07)
Alcaligenes denitrificans Y2k-2 was obtained by selective enrichment followed by screening from soil samples, which showed omega-amino acid:pyruvate transaminase activity, to kinetically resolve aliphatic beta-amino acid, and the corresponding structural gene (aptA) was cloned. The gene was functionally expressed in
J S Shin et al.
Bioscience, biotechnology, and biochemistry, 65(8), 1782-1788 (2001-10-02)
Microorganisms that are capable of (S)-enantioselective transamination of chiral amines were isolated from soil samples by selective enrichment using (S)-alpha-methyl-benzylamine ((S)-alpha-MBA) as a sole nitrogen source. Among them, Klebsiella pneumoniae JS2F, Bacillus thuringiensis JS64, and Vibrio fluvialis JS17 showed good
K Yonaha et al.
The Journal of biological chemistry, 267(18), 12506-12510 (1992-06-25)
The complete amino acid sequence of bacterial omega-amino acid:pyruvate aminotransferase (omega-APT) was determined from its primary structure. The enzyme protein was fragmented by CNBr cleavage, trypsin, and Staphylococcus aureus V8 digestions. The peptides were purified and sequenced by Edman degradation.
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