Metabolic Coupling in Cellular Energy Dynamics

University:
Swansea University
Course:
PM-133 | Evolutionary and Molecular Genetics
Academic year:

2023
Views:

122

Pages:

4
Author:

Amal J.

Metabolic Couplingcoupling of a non spontaneous reaction with a spontaneousreaction.AG°[P]change infree energyG= AG + 2.303 Rt log[R]at standard conditionRGas constant 8.31J trol.kAtequilibrium AG=0T Temperature.[P]O=AG't o 2.303 RT log[R]atequilibrium,log[P] = KeqEquilibrium constant.[R] Considering a reversible reactionTheABifforward reaction spontaneous (A B) backward (139)will be non-sportSpeed/Rat of Enzyme Catalysisstudy of rate of enzyme catalysis Enzyme catalysis kinetics.RP rate Vostorder reactionVo a [R]rateofreaction a Conc of Reactant.Vo= K[R]K=rateconstantK1KzE+SESE+P Slowest Step- DeterminesK-1K-2Rate of a reactionTransitionHere, K2- rate of stocstatestep.Vo = K2 [ES] [ [ES] }cannot be determined since it's transition state](I)rateof formation of ESVo = Kg [E][s]= K1 [[E7][Es]][s]= K112 Rate of breakdown of ESNo = Kz [ES] + K-I [ES]= [ES]2 at steady state,Rate of formation of ES = Rate of breakdown ofES.K,[[ET][s] - [ES][s]] = [Es][K2+k-1][1ET][s] - [ES][s]] = (K2+ K-1)Km - Michaelis Menter's[Es]. (K1)constant[ET] [s] - [Es][s][Es][Es][ET][s] - [s] = KM3[Es][Es] = [ET][s]4KM+[s]5Vo = K2 Es4in5Vo = K2 [ET][s]6KM+[s]At high conc of S, , all active site of enzymes are filled withsubstrateRate Vo = VmaxET= EsVmax =K2[ET]717 in 6Vo = Vmax[s]KM+[s] 1- 12Vmax = Vmax [s]28kmg + [s]Km + [sJ= %[S]Km = [s]