Origin of Glycine from Acid Hydrolysis of the β-Lactam Antibiotic A16886B

Author:

Brannon D. R.1,Mabe J. A.1,Ellis R.1,Whitney J. G.1,Nagarajan R.1

Affiliation:

1. The Lilly Research Laboratories, Eli Lilly & Co., Indianapolis, Indiana 46206

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.

Publisher

American Society for Microbiology

Subject

Infectious Diseases,Pharmacology (medical),Pharmacology

Reference6 articles.

1. Synthesis of D. 6-amino-B-carboxyvaleramide;Abraham E. P.;Biochem. J.,1954

2. The biosynthesis of penicillin. 2. The incorporation of cystine into penicillin;Arnstein H. R. V.;Biochem. J.,1954

3. The decarboxylation of amino acids, proteins, and peptides by N-bromosuccinimide;Chappelle E. W.;J. Biol. Chem.,1957

4. Further degradation products of cephalosporin C;Jeffery J.;Biochem. J.,1960

5. ft-Lactam antibiotics from Streptomyces;Nagarajan R.;J. Amer. Chem. Soc.,1971

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