The absolute configuration of the amino acids in delta-(alpha-aminoadipyl)cysteinylvaline from Penicillium chrysogenum.
Radioactive carbon-14 L-alpha-aminoadipic acid, L-cysteine, or L-valine were readily incorporated into the intracellular tripeptide, delta-(alpha-aminoadipyl)cysteinylvaline (ACV), by washed starved cells of Penicillium chrysogenum. The labeled ACV in each case was oxidized with performic acid and isolated as its corresponding sulfonic acid derivative. After acid hydrolysis, the configuration of the component acids was determined by L- and D-amino acid oxidases, which showed the tripeptide (ACV) from P. chrysogenum to be delta-(L-aminoadipyl)-L-cysteinyl-D-valine.
D015074:2-Aminoadipic Acid; D000594:Amino Acid Oxidoreductases; D003545:Cysteine; D003605:D-Amino-Acid Oxidase; D009842:Oligopeptides / Q000032:analysis; D010407:Penicillium / Q000032:analysis*; D010408:Penicillium chrysogenum / Q000032:analysis*; D011487:Protein Conformation; D013237:Stereoisomerism; D014633:Valine
D009842:Oligopeptides; D015074:2-Aminoadipic Acid; D000594:Amino Acid Oxidoreductases; D003605:D-Amino-Acid Oxidase; D014633:Valine; D003545:Cysteine