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- W184742874 abstract "Kynurenine-α-ketoglutarate aminotransferase has been purified and crystallized from a cell-free extract of Hansenula schneggii grown in the medium containing 0.15% L-tryptophan. The crystalline enzyme was found to be homogeneous upon ultracentrifugation and disc gel electrophoresis. The molecular weight was determined to be about 100,000. The enzyme consists of two subunits identical in molecular weight (56,000). The enzyme exhibits absorption maxima at 280, 335 and 435 nm, and contains about two moles of pyridoxal 5'-phosphate per mole of enzyme. The enzyme-bound pyridoxal 5′-phosphate shows the negative circular dichroic bands in contrast with other pyridoxal 5′-phosphate enzymes acting on L-amino acids. In addition to L-kynurenine, which is the most preferred substrate, various other L-amino acids, e.g. L-3-hydroxykynurenine, L-tryptophan, L-valine, L-α-aminoadipate and L-methionine serve as the amino donors for α-ketoglutarate. α-Ketoglutarate, α-ketoisocaproate, β-phenylpyruvate and α-ketocaproate are the good amino acceptors for L-kynurenine. The enzyme activity is significantly affected by both the carbonyl and sulfhydryl reagents. The enzyme is also inhibited by dicarboxylic acids such as adipate and pimelate. KEYWORDS Kynurenine aminotransferase;, Hansenula schneggii;, pyridoxal 5′-phosphate;, circular dichroic bands;, L-kynurenine;, L-tryptophan;, α-ketoglutarate;, substrate specificity." @default.
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- W184742874 date "1981-01-01" @default.
- W184742874 modified "2023-10-04" @default.
- W184742874 title "KYNURENINE AMINOTRANSFERASE WITH LOW SUBSTRATE SPECIFICITY OF HANSENULA SCHNEGGII" @default.
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- W184742874 doi "https://doi.org/10.1016/b978-0-08-025382-4.50073-3" @default.
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