University:
University of Wolverhampton
Course:
4PY019 | Pharmacy
Academic year:

2024
Views:

175

Pages:

3
Author:

Sara

Amino acids and enzyme kinetics Study online at https://quizlet.com/_d97q30 Aliphatic non-polar amino acids -Glycine (G) -Alanine (A) -Proline (P) -Leucine (L) -Isoleucine (I) -Methionine (M) -Valine (V) Aromatic non-polar amino acids phenylalanine, tryptophan aliphatic hydroxyl amino acids serine and threonine acidic amino acids aspartate, glutamate Amidic Amino Acids asparagine, glutamine basic amino acids lysine, arginine, histidine Sulfur amino acids cysteine and methionine Imino acid Proline optical activity all optically active except gly Only L configuration amino acids are incorporate into proteins Where are D-amino acids found? some antibiotics and bacterial cell walls zwitterions in low pH carboxyl group accepts proton molecule becomes positive Zwitterions high pH Amine group loses proton proton molecule becomes negative cofactors metal or small organic molecules coenzymes organic cofactors when tightly bound called prosthetic group when loosely bound called cosubstrate Oxidoreductases catalyze oxidation-reduction reactions Tranferases transfer functional groups Hydrolases hydrolysis reactions lyases add groups to or remove groups from double-bonded substrates 1/3 Amino acids and enzyme kinetics Study online at https://quizlet.com/_d97q30 isomerases Transfer of groups within molecules to yield isomeric forms ligases bond formation coupled with ATP hydrolysis Vmax maximum initial velocity or rate of an enzyme-catalysed reaction as all active sites are occupied Michaelis-Menten equation v = (vmax [S])/(Km + [S]) Km Substrate concentration at 1/2 Vmax How much concentration needed for significant catalysis measured in M turnover number of an enzyme Vmax = K2[E]T number of substrate molecules convertedinto product by an enzyme molecule in a unit time when the enzyme is fullysaturated with substrate catalytic efficiency equation Kcat/Km X [S][E] Factors affecting Km Substrate, temperature, pH and ionic strength Increasing Km Decreases affinity for formation of enzyme substrate complex line weaver burk equation 1/v0 = (Km/Vmax)(1/[S]) + 1/Vmax competitive inhibition Active site binding reversible increases Km Doesn't affect Vmax Non-competitive inhibition Allosteric site binding reversible or non reversible Km unchanged Vmax decreased Allosteric enzymes Do Not Obey Michaelis-Menten Kinetics Binding of an enzyme can affect another active site on the enzyme 2/3 Amino acids and enzyme kinetics Study online at https://quizlet.com/_d97q30 Homotropic allostery Binding of identical molecules in a co-operative manner heterotropic allostery Co-operative binding of other substances 3/3