77087
ω-Transaminase, Aspergillus fumigatus
recombinant, expressed in E. coli, ≥0.20 U/mg
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About This Item
Número de CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
Productos recomendados
recombinant
expressed in E. coli
form
powder
specific activity
≥0.20 U/mg
storage temp.
−20°C
Packaging
Bottomless glass bottle. Contents are inside inserted fused cone.
Unit Definition
1 U corresponds to the amount of enzyme which releases 1 μmol acetophenone per minute at 30°C. (R(−)-α-methyl-benzylamine as substrate).
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1 - Skin Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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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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
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.
Applied microbiology and biotechnology, 61(5-6), 463-471 (2003-04-11)
A transaminase from Vibrio fluvialis JS17 showing activity toward chiral amines was purified to homogeneity and its enzymatic properties were characterized. The transaminase showed an apparent molecular mass of 100 kDa as determined by gel filtration chromatography and a subunit
N Watanabe et al.
Journal of biochemistry, 105(1), 1-3 (1989-01-01)
The three-dimensional structure of omega-amino acid:pyruvate aminotransferase from Pseudomonas sp. F-126, an isologous alpha 4 tetramer containing pyridoxal 5'-phosphate (PLP) as a cofactor, has been determined at 2.0 A resolution. The diffraction data were collected with a newly developed Weissenberg
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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