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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Extra info for Biochemistry and Molecular Biology of Antimicrobial Drug Action
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.