Antibiotics: Containing the Beta-Lactam Structure by E. P. Abraham (auth.), Professor Dr. Arnold L. Demain, Ms.

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By E. P. Abraham (auth.), Professor Dr. Arnold L. Demain, Ms. Nadine A. Solomon (eds.)

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Collected Papers of P.L. Kapitza: U.S.S.R. Academy of Sciences, F.R.S., Volume 1

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Coli decompose the antibiotic to penicilloic acid (TAMURA et al. 1976). On the other hand, the Streptomyces carboxypeptidase R61 (FRERE et al. 1975a, b) and the carboxypeptidase of B. stearothermophilus (HAMMARSTROM and STROMINGER 1975) decomposes bound penicillin to phenylacetylglycine and a thiazoline derivative. The first reaction is obviously identical to that catalyzed by p-lactamases. The physiological significance of the second type of fragmentation (Fig. 6) is not known although fragmentation products might be utilized and the '-CH2-C-NH~S+CH3 O II I' N CH3 o C o~1 o ~ ~-CH2-C-NH-'--(S)< - 8 6 NTCOOH O~\ OH penicilloic acid COOH ~ '-CH -C-NH-CH2 O- 2 8 b o~\ OH phenylacetyl-glycine o CH3 + ~,H \ Sr.

In fact, the PBP pattern may provide corroborating evidence for the taxonomic classification of bacteria. , highest molecular size on the gel). Thus PBP 1 of E. coli need not have anything in common with PBP 1 of gonococci. Nevertheless, a more detailed comparison of PBPs, by a variety of functional criteria, suggests that within the group of Enterobacteriaceae, at least some of the PBPs of comparable molecular size may have similar physiological functions as well (GEORGOPAPADAKOU and LID 1980; NOGucm et al.

Correspondingly, the optimal substrates with the R61 enzyme contained the free amino group on a glycine, while good acceptors for the R39 enzyme contained the aminogroup on a meso-diaminopimelic acid residue (Fig. 5). f) Differences Among the Model Enzymes The various penicillin-sensitive enzymes studied could be grouped into a series of proteins representing a gradually increasing specificity for the structure of the acceptor nucleophile. Thus, the S. albus G enzyme had exclusively hydrolytic (D,D carboxypeptidase and endopeptidase) activities.

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