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重组
expressed in E. coli
表单
powder
比活
≥0.5 U/mg
储存温度
2-8°C
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生化/生理作用
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.
包装
Bottomless glass bottle. Contents are inside inserted fused cone.
单位定义
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)
警示用语：
Danger
危险声明
危险分类
Resp. Sens. 1 - Skin Sens. 1
储存分类代码
13 - Non Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
新产品
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
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
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.
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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