Romox-500 Capsule

Amoxicillin like other penicillin, inhibit the penicillin binding proteins (PBPs {specifically PBP-1A}), which are transmembrane surface enzymes that catalyze the cross linking (transpeptidation) between the peptidoglycans in the bacterial cell wall. Amoxicillin is able to bind to the PBPs by geometrically mimicking the natural D-alanyl-D-alanine substrate that is generally bound to the enzyme. By substituting itself for D-alanyl-D-alanine, the appropriate strands needed for cross-linking are not available and the cell wall biosynthesis process is left incomplete. It also acylates the penicillin-sensitive transpeptidase C-terminal domain by opening the lactam ring. This inactivation of the enzyme prevents the formation of a cross-link of two linear peptidoglycan strands, inhibiting bacterial cell wall synthesis. Cell lysis is then mediated by bacterial cell wall autolytic enzymes such as autolysins or murein hydrolases; it is possible that amoxicillin interferes with an autolysin inhibitor. In gram negative bacteria the outer membrane of cell wall comprises of lipopoly saccharides with narrow porin channels which function as barriers to permeability of beta-lactam antibiotics.But amoxicillin being hydrophilic can diffuse through these porin channels more swiftly and significantly than other natural penicillins and show activity against gram negative bacteria also. Beta- Lactam antibiotics including amoxicillin kill bacterial cells only when they are actively growing and synthesizing cell wall.