title: Origin of glycine from acid hydrolysis of the  -lactam antibiotic A16886B.
abstract: Structural analysis of two new beta-lactam antibiotics, A16884A and A16886B, indicated that they, like cephalosporin C, were composed of modified valine and cysteine residues, and alpha-aminoadipic acid. However, acid hydrolysis of A16886B and A16884A produced three times as much glycine as did hydrolysis of cephalosporin C under the same conditions. Samples of A16886B-(14)C-6 and A16886B-(14)C-8 were prepared by the addition of cysteine-(14)C-3 and cystine-(14)C-1 to fermentations of Streptomyces clavuligerus. The specific activity of glycine obtained from hydrolysis of A16886B-(14)C-6 was considerably higher than that from hydrolysis of A16886B-(14)C-8. An explanation for the difference in amounts of glycine obtained from hydrolysis of these antibiotics is discussed.
mesh_terms: D002219:Carbamates; D002247:Carbon Isotopes; D002511:Cephalosporins / Q000302:isolation & purification; D002854:Chromatography, Paper; D003653:Decarboxylation; D005998:Glycine / Q000138:chemical synthesis*; D006868:Hydrolysis; D007202:Indicators and Reagents; D008738:Methyl Ethers; D013302:Streptomyces
chemical_list: D002219:Carbamates; D002247:Carbon Isotopes; D002511:Cephalosporins; D007202:Indicators and Reagents; D008738:Methyl Ethers; D005998:Glycine