77087
ω-Transaminase, Aspergillus fumigatus
recombinant, expressed in E. coli, ≥0.20 U/mg
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10 MG
$102.00
50 MG
$387.00
About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
$102.00
Check Cart for Availability
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recombinant
expressed in E. coli
Quality Level
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
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omega-Amino acid-pyruvate aminotransferase.
K Yonaha et al.
Methods in enzymology, 143, 500-504 (1987-01-01)
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.
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
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