93006
ω-Transaminase, Neosartorya fischeri
recombinant, expressed in E. coli, ≥0.4 U/mg
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About This Item
Número CAS:
Código UNSPSC:
12352204
NACRES:
NA.54
Produtos recomendados
recombinante
expressed in E. coli
Nível de qualidade
Formulário
powder
atividade específica
≥0.4 U/mg
temperatura de armazenamento
−20°C
Embalagem
Bottomless glass bottle. Contents are inside inserted fused cone.
Definição da unidade
1 U corresponds to the amount of enzyme which releases 1 μmol acetophenone per minute at 30°C. (R(−)-α-methyl-benzylamine as substrate).
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Resp. Sens. 1 - Skin Sens. 1
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°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.
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
Beta alanine aminotransferase (s) from a plant source.
R A Stinson et al.
Biochemical and biophysical research communications, 34(1), 120-127 (1969-01-06)
T P West
Antonie van Leeuwenhoek, 77(1), 1-5 (2000-03-04)
A determination of the possible role of the salvage enzyme cytosine deaminase or beta-alanine-pyruvate transaminase in the catabolism of the pyrimidine bases uracil and thymine by the opportunistic pathogen Burkholderia cepacia ATCC 25416 was undertaken. It was of interest to
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
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