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

ISBN-10: 3642819664

ISBN-13: 9783642819667

ISBN-10: 3642819680

ISBN-13: 9783642819681

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Additional info for Antibiotics: Containing the Beta-Lactam Structure

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1966). , an endopeptidase reaction). All three reactions were sensitive to penicillin (IZAKI et al. 1966). Subsequently, the same types of penicillin-sensitive enzyme reactions were detected in a large number of other bacterial species (IZAKI et al. 1968; ARAKI et al. 1966; LINNETT and STROMINGER 1974a, b; PELLON et al. 1976; WICKUS and STROMINGER 1972a; WICKUS and STROMINGER 1972 b). The basic similarity between the carboxypeptidase and transpeptidase reactions has been recognized: in both cases the carbonyl of the penultimate Dalanine is transferred to an exogenous nucleophile.

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. 1979; CURTIS et al. 1979a,b). The quantitative distribution of bound penicillin among the PBPs differs from one bacterium to another. Assuming monovalent binding, one can estimate the approximate number of molecules of various PBPs per cell and also the fraction of total membrane protein represented by the PBPs.

Coli (left side) and an Archaebacterium. M, N-acetylmurarnic acid; G, N-acetylglucosamine; Tal, N-acetyl talosarninouronic acid. Black arrows indicate the two main repeating chemical bonds in the cell wall of E. coli: the fJ-l,4 glycosidic bonds (A) and the transpeptide bonds (B). The white arrows indicate the sites of attack of hydrolytic enzymes identified in E. coli: amidase (1); transglycosylase (2); glucosarninidase (3); L,D carboxypeptidase (4); D,D carboxypeptidase (5); and endopeptidase (6).

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


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