Biochemistry and Molecular Biology of Antimicrobial Drug by Trevor J. Franklin, George Alan Snow

By Trevor J. Franklin, George Alan Snow

The topic is one in all significant curiosity in easy microbiology and infectious illnesses and the publication is a recognized vintage.

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1 Properties of penicillin-binding proteins of Escherichia coli Protein no. Molecular wt (kDa) Enzyme activities 1a 91 1b 91 2 66 3 60 4 49 Transpeptidase Transglycosylase Transpeptidase Transglycosylase Transpeptidase Transglycosylase Transpeptidase Transglycosylase DO-Carboxypeptidase 5 41 Do-Carboxypeptidase 6 40 Do-Carboxypeptidase transpeptidase activities, borne respectively by the non-penicillin-binding and penicillin-binding modules. PBPs 1a and 1b of Escherichia coli exemplify this bifunctional type and are described as Class A PBPs.

Threonine and the number of residues can vary from one to five. In Type Al peptidoglycans the Llysine of the Type II peptide side chain is usually replaced by meso-2,6-diaminopimelic acid, and there is no bridging group. Cross-linking occurs 24 between the D-alanine of one side chain and the 6amino group of the diaminopimelic acid of another. This peptidoglycan type is characteristic of many rod-shaped bacteria, both the large family of Gram-negative rods and the Gram-positive bacilli. Structure and biosynthesis of peptidoglycan In the less common Type B peptidoglycans crosslinkage occurs between the a-carboxyl group of the o-glutamic acid of one peptide side chain and the o-alanine of another, through a bridge containing a basic amino acid.

The next two residues are o-glutamic acid and then L-Iysine. The lysine, however, is attached through its a-amino group to the ,),-carboxyl group of the glutamic acid. The a-carboxyl group of the glutamic acid is amidated at a later stage in the biosynthesis, so the second amino acid residue is sometimes referred to as o-isoglutamine. The biosynthesis of the pentapeptide is completed by addition not of an amino acid but of a dipeptide, o-alanyl-o-alanine, which is separately synthesized. A racemase acting on L-alanine gives o-alanine, and a ligase then joins two molecules, giving the dipeptide.

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