CHEM357 Chapter Notes - Chapter 10: Hemoglobin, Enzyme Inhibitor, Rate Equation
30 May 2017
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Can be proteins or rna enzymes (ribozymes) Applies to many enzymes e. g. chymotrypsin, hydrolyzes amide linkages of polypeptides. In early days of enzymology, hard to measure [enzyme] (typically ~10-10-10-8m) therefore focused on changes in [substrate] and [product] (~10-6-10-3m) Henri (1902), michaelis & menten (1913), and briggs & haldane (1925) developed the kinetic formulation: E = free enzyme and s = free substrate are hard to measure. Rewrite equation in terms of measurable eo = total enzyme and so = total substrate. 0 where km = (k-1 + k2)/k1 = michaelis constant for a given e, s combination. Vmax = k2 eo kcat eo and kcat=catalytic constant or turnover number. Consider limiting cases: when so << km, when so >> km, when so = km. Validity of steady state approximation in mm kinetics: A. cornish-bowden, fundamentals of enzyme kinetics (1979) p 24-5. Vo reduces to expression obtained using ssa when sk o.
