93006
ω-Transaminase, Neosartorya fischeri
recombinant, expressed in E. coli, ≥0.4 U/mg
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About This Item
Productos recomendados
recombinant
expressed in E. coli
form
powder
specific activity
≥0.4 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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omega-Amino acid-pyruvate aminotransferase.
Methods in enzymology, 143, 500-504 (1987-01-01)
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.
Biochemical and biophysical research communications, 34(1), 120-127 (1969-01-06)
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
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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