Biosynthesis of Edeine (cas 11006-90-9): Fractionation and characterization of enzymes responsible for biosynthesis of Edeine (cas 11006-90-9) A and B
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Add time:08/20/2019 Source:sciencedirect.com
Enzymes obtained from cells disrupted by lysozyme treatment were resolved into three complementary enzyme fractions by DEAE-cellulose-Sephadex G-200 chromatography. These enzymes of molecular weight 210 000 (A), 180 000 (B) and 100 000 (C) were responsible for the activation of the constituent amino acids of Edeine (cas 11006-90-9)s and their subsequent polymerization into biologically active peptides.Two of these fractions 210 000 and 180 000 molecular weight contained covalently bound pantetheine.Fraction A of 210 000 mol. wt activated β-tyrosine, whereas Fraction B of 180 000 mol. wt activated diaminopropionic acid, isoserine, 2,6-diamino-7-hydroxyazelaic acid and glycine. Fraction C of 100 000 mol. wt, which predominately activated diaminopropionic acid and isoserine, was inactive for β-tyrosine. The amino acid activation was measured by ATP-32PPi exchange. All three enzyme fractions were present in extracts obtained from cells of late logarithmic and early stationary phase of growth (8–12 h). Enzymes of old cells (20–24 h) resolved into two fractions only, of 210 000 and 160 000 molecular weight. Both have shown the catalytic activity for the same edeine constituent amino acids as Fraction A and B.Fractions A and B formed complexes with constituent amino acids of edeines which were precipitable with trichloroacetic acid. The amino acids in these complexes were covalently bound to the protein.
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