Biosynthesis of trans-4-hydroxy-L-proline by Streptomyces griseoviridus.
Radioisotopic experiments have revealed that free trans-4-hydroxy-L-proline is an intermediate synthesized from L-proline during formation of the peptide-bound cis-4-hydroxy-D-proline residue in the antibiotic, etamycin. This conclusion was based on the fact that 1) both radiolabeled L-proline and trans-4-hydroxy-L-proline are precursors of the bound D-imino acid as noted previously by Hook and Vining ((1973) J. Chem. Soc. Chem. Commun. 185-186; (1973) Can. J. Biochem. 51, 1630-1637), 2) the unlabeled trans isomer specifically inhibited the incorporation of radiolabel from proline into the antibiotic, 3) the 14C-hydroxyimino-acid was isolated from the intracellular pool and medium following incubations with L-[14C]proline during antibiotic biosynthesis and when etamycin synthesis was blocked by D-leucine. By means of chromatographic and enzymatic analyses, it was established that the free imino acid possesses the trans-L configuration.
D000596:Amino Acids / Q000378:metabolism; D002250:Carbon Radioisotopes; D002701:Chloramphenicol / Q000494:pharmacology; D006909:Hydroxyproline / Q000096:biosynthesis*; D007536:Isomerism; D007553:Isotope Labeling; D007700:Kinetics; D010452:Peptide Biosynthesis; D011691:Puromycin / Q000494:pharmacology; D013302:Streptomyces / Q000187:drug effects / Q000378:metabolism*; D014316:Tritium
D000596:Amino Acids; D002250:Carbon Radioisotopes; D014316:Tritium; D011691:Puromycin; D002701:Chloramphenicol; D006909:Hydroxyproline