EC Number   |
Application |
Reference |
|---|
    2.6.1.1 | biotechnology |
an enzymatic method for the synthesis of the amino acid Phe is developed. AAT from porcine heart is immobilized by covalent attachment and entrapment, and the resulting immobilized preparations are compared to the soluble enzyme both in terms of stability and reaction efficiency |
721515 |
| 2.6.1.1 | medicine |
following doxorubicin administration, triple-negative breast cancer cells, which do not express the estrogen receptor, the progesterone receptor, and the human epidermal growth factor receptor, acquire metabolic alteration, causing increased glutamine flux for the synthesis of aspartate which can be converted into oxaloacetate by GOT1. Subsequently, this oxaloacetate is converted into malate and then pyruvate, maintaining the NADP+/NADPH ratio which neutralizes doxorubicin-induced oxidative stress. Repression of GOT1 results in doxorubicin-induced formation of reactive oxygen species, thereby increasing doxorubicin sensitivity |
737616 |
| 2.6.1.1 | medicine |
the inhibitor of C-S lyase, aminooxyacetic acid hemihydrochloride, reduces renal injuries due to cisplatin in rats. On day 5 following a bolus cisplatin injection, in vivo nephrotoxic potentials are in the decreasing order of species rats > mice, rabbits, based on body surface. The levels of renal Pt residue at the nephrotoxic dose are in order of rabbits > rats > mice. The activity of endogenous basal mitochondrial aspartate aminotransferase, one of the C-S lyases, in the renal cortex of naive animals is rats > mice, rabbits. Expression of mitochondrial C-S lyase in the kidney is observed at approximately 37 kDa in all five species used. In in vitro studies, the cytotoxicity of cisplatin is dependent on the expression level of C-S lyase mRNA in the respective renal cells |
-, 715070 |
| 2.6.1.1 | synthesis |
codon-optimized expression in Escherichia coli with His6-tag and purification. The enzyme activity of purified aspartate aminotransferase reaches 150000 U/l. The preparation shows high stability during long-term storage at -20ºC |
738861 |
| 2.6.1.1 | synthesis |
expression in 2-phenylethanol producing strain Saccharomyces cerevisiae YS58, and use of the strain for the coproduction of 2-phenylethanol and L-homophenylalanine via a fermentation process. The L-homophenylalanine productivity of the recombinant Saccharomyces cerevisiae improves by 78.9% in comparison to the wild-type. High yields of 43.7 mM L-homophenylalanine and 32.4 mM 2-phenylethanol are achieved |
-, 738727 |
| 2.6.1.1 | synthesis |
mutant enzyme R292E/L18H can use L-lysine as inexpensive amino donor for the production of L-homophenylalanine. The low solubility of product L-homophenylalanine and spontaneous cyclization of 2-keto-6-aminocaproate drive the reaction completely towards production of L-homophenylalanine |
658335 |
