Origin of Glycine from Acid Hydrolysis of the β-Lactam Antibiotic A16886B
Open Access
- 1 March 1972
- journal article
- research article
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 1 (3) , 242-246
- https://doi.org/10.1128/aac.1.3.242
Abstract
Structural analysis of two new β-lactam antibiotics, A16884A and A16886B, indicated that they, like cephalosporin C, were composed of modified valine and cysteine residues, and α-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.Keywords
This publication has 6 references indexed in Scilit:
- Incorporation of Labeled Precursors into A16886B, a Novel β-Lactam Antibiotic Produced by Streptomyces clavuligerusAntimicrobial Agents and Chemotherapy, 1972
- .beta.-Lactam antibiotics from StreptomycesJournal of the American Chemical Society, 1971
- Further degradation products of cephalosporin C. Isolation and synthesis of 2-(4-amino-4-carboxybutyl)thiazole-4-carboxylic acidBiochemical Journal, 1960
- THE DECARBOXYLATION OF AMINO ACIDS, PROTEINS, AND PEPTIDES BY N-BROMOSUCCINIMIDEJournal of Biological Chemistry, 1957
- Synthesis of d-δ-amino-δ-carboxyvalerylglycine (a degradation product of cephalosporin N) and of dl-δ-amino-δ-carboxyvaleramideBiochemical Journal, 1954
- The biosynthesis of penicillin. 2. The incorporation of cystine into penicillinBiochemical Journal, 1954