B2549
Branched-chain amino acid transaminase bacterial
recombinant, expressed in E. coli, lyophilized powder, ≥2 units/mg protein (biuret)
recombinant
expressed in E. coli
form
lyophilized powder
specific activity
≥2 units/mg protein (biuret)
storage temp.
2-8°C
Other Notes
One unit will convert 1.0 μmole of 2-ketoisovalerate to L-valine per min at pH 7.0 at 37 °C in the presence of L-glutamate and pyridoxal phosphate.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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L W Tremblay et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 65(Pt 11), 1071-1077 (2009-11-20)
Unlike mammals, bacteria encode enzymes that synthesize branched-chain amino acids. The pyridoxal 50-phosphate-dependent transaminase performs the final biosynthetic step in these pathways, converting keto acid precursors into -amino acids. The branched-chain amino-acid transaminase from Mycobacterium tuberculosis (MtIlvE) has been crystallized
Gregory S Maloney et al.
Plant physiology, 153(3), 925-936 (2010-05-04)
Branched-chain amino acids (BCAAs) are synthesized in plants from branched-chain keto acids, but their metabolism is not completely understood. The interface of BCAA metabolism lies with branched-chain aminotransferases (BCAT) that catalyze both the last anabolic step and the first catabolic
Kavitha Gowda et al.
Journal of neurochemistry, 117(2), 309-320 (2011-02-04)
Excised retinas from euglycemic and diabetic Sprague-Dawley rats were studied to evaluate differences in glutamate metabolism related to diabetes. Reports suggest, neuronal cell death possibly caused by glutamate excitotoxicity, is an early consequence of diabetes. To monitor the influence of
Andrej Kochevenko et al.
Journal of plant physiology, 169(5), 437-443 (2012-01-10)
Although the branched-chain amino acids (BCAAs) are essential components of the mammalian diet, our current understanding of their metabolism in plants is still limited. It is however well known that the branched-chain amino acid transaminases (BCATs) play a crucial role
Thierry Gefflaut et al.
Methods in molecular biology (Clifton, N.J.), 794, 55-72 (2011-10-01)
Aminotransferases are key enzymes of the metabolism of proteinogenic amino acids. These ubiquitous biocatalysts show high specific activities and relaxed substrate specificities making them valuable tools for the stereoselective synthesis of unnatural amino acids. We describe here the application of
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