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Enzyme regulation, hemoglobin vs. myoglobin, kinetics of allosteric enzymes

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Colorado State University
Life Science
LIFE 210
Paul Laybourn

9 September General Enzyme Regulation Two main ways Expression, protein level – takes minutes to hours Enzyme activity – takes seconds Conformational changes Affects ability to reduce ΔG‡ - k and K cat M In response to Substrate binding Effector binding – bind site separate from active site Generally referred to as “ligands” Regulated enzymes often have sigmoidal kinetics Greek “Allos” – other; “Stereos” – shape Homoallostery – substrate is effector Heteroallostery – non substrate effector Hemoglobin T – tight state, binds BPG & CO m2re tightly R – relaxed state, binds O 2ore tightly Relaxed is higher affinity Hemoglobin vs. myoglobin Myoglobin (Mb) – monomer Hemoglobin (Hb) – heterotetramer Hb also regulated by Lower pH – stabilizes “T” CO – C-terminus modification stabilizes “T” 2 BPG – binds and stabilizes “T” Hb has cooperativity in binding (since it has 4 monomers) Positive linkage – both substrates bind the same conformation more tightly, cooperativity Negative linkage can occur as well Kinetics of Allosteric Enzymes Sigmoidal vs. Hyperbolic (M – M) Kinetics Sigmoidal kinetics is not Michaelis – Menton kinetics
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