Notes in CBB24 enzyme kinetics

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Published	09/14/2024	Gibbs free energy change (ΔG)  •is the free energy change between the {{c1::products}} and the {{c1::reactants}} •reflects the direction of …
Published	09/14/2024	Describing Reaction VelocityThe rate of a chemical reaction (velocity) can be described by determining how quickly {{c1::reactants (substrates)}} are …
Published	09/14/2024	The initial velocity (Vo ) is the rate at the {{c1::initial}} stage of the reaction.
Published	09/14/2024	Enzyme Kinetics of One Substrate ReactionoIn the kinetic study of an enzyme-catalyzed reaction, the reaction {{c1::velocity}} (Vo) is plotted against …
Published	09/14/2024	Michaelis-Menten KineticsoThe {{c1::enzyme (E)}} reversibly binds to its {{c1::substrate}} to form an {{c2::ES complex}}. oThe substrate is converted…
Published	09/14/2024	Michaelis-Menten KineticsEquation for Vo?{{c1::}}oMM equation describes how the rate of the reaction dependent  on both the enzyme [E] and the su…
Published	09/14/2024	Michaelis-Menten PlotDescribes the relationship between {{c1::[S]}} and the {{c1::reaction velocity (Vo)}} determined in the presence of a {{c2:…
Published	09/14/2024	Michaelis-Menten Plot--> VmaxoVmax is directly proportional to the {{c1::enzyme}} concentration!!!!!!o So, the only way to Vmax increases is throug…
Published	09/14/2024	Michaelis-Menten Plot--> Vmax--> clinical correlateoPhenylketonuria (PKU): • a genetic disorder caused by mutations leading deficiency of phenyl…
Published	09/14/2024	Michaelis-Menten Plot--> Km• reflects the {{c2::affinity}} of the enzyme for a substrate. •does not change with the concentration of enzyme or sub…
Published	09/14/2024	Michaelis-Menten Plot--> KmA. {{c1::Small (low)}} Km:Reflects a {{c2::high}} affinity of the enzyme for substrate.Indicates that a {{c3::low}} conc…
Published	09/14/2024	GLUT1 and GLUT3Km of GLUT1 and GLUT3 is approximately 1mM; thus, they have a {{c1::high}} affinity for glucose.Because the basal blood glucose level i…
Published	09/14/2024	Michaelis-Menten Plot --> Km --> Physiologic SignificanceHexokinase IIn red blood cells (erythrocytes)Has a Km for glucose of ~ 0.05 mMThe {{c1:…
Published	09/14/2024	Double-Reciprocal Plot (Lineweaver-Burk Plot)If {{c1::1/Vo}} is plotted against {{c2::1/[S]}}, a straight line is obtained.The equation of the line is…
Published	09/14/2024	Order of Enzyme-Catalyzed ReactionsFirst Order:When [S] {{c1::<<<}} KmThe velocity of the reaction is {{c3::proportional}} to the substrate c…
Published	09/14/2024	Turnover number (kcat)Vmax = kcat[E]t -->kcat={{c1::}}•Number of substrate molecules “turned over” per time (in one second) •  Reciprocal is t…
Published	09/14/2024	Catalytic efficiency= {{c1::kcat/Km}}- Measure of efficiency indicates how well enzyme works at {{c2::low}} substrate concentration.- can be increased…
Published	09/14/2024	Cooperative Enzyme Kineticso show a {{c1::sigmoidal}} kinetics  oCooperative enzymes (a.k.a. {{c2::allosteric}} enzymes) can be induced to c…
Published	09/14/2024	Allosteric regulationoTwo types of allosteric regulations ({{c1::activation}} and {{c1::inhibition}})
Published	09/14/2024	Allosteric regulation--> allosteric inhibition•Occurs when an allosteric inhibitor (a.k.a. allosteric negative effector) binds to an enzyme, • and …
Published	09/14/2024	Allosteric regulation--> allosteric activation•Occurs when an allosteric activator (a.k.a. positive effector) binds to locations on an enzyme other…
Published	09/14/2024	Allosteric regulation--> clinical correlateExample: {{c1::GOUT}} oCharacterized by inflammation and accumulation of uric acid crystal in joints of …
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