ABSTRACT
In a long-chain peptide composed of l-amino acid residues, intramolecular hydrogen bonding leads to a right-handed helix, where the hydrogen atom on the amide nitrogen is hydrogen-bonded to the oxygen of the carbonyl on the fourth amino acid residue. There is a single covalent bond between the two -Ç-bonds, so it is not possible draw a resonance form involving the orbitals of the -Ç-bonds without introducing charges into the molecule. The purpose of binding into a reactive complex is to weaken key substrate bonds to facilitate the desired chemical reactions. Penicillin G catalyzes the cross-linking reaction between peptidoglycan molecules. Enzyme kinetics for a single substrate with a hyperbolic rate substrate concentration are described by the Michaelis-Menten equation, where Km is the Michaelis constant, [S] is the substrate concentration, V is the rate of the reaction, and Vmax is the reaction rate when the substrate concentration approaches infinity.
