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Enzymes 3, Bioenergetics Free Energy Std. Free Energy ΔG°=-2.3RT*log(Keq) ~-1.4logKeq reactants, products []=1M low Keq, ΔG°ɬ high Keq, ΔG°ɘ, Enzyme Regulation Covalent Modification Phosphorylation by kinases X-OH+ATP->X-OPO3+ADP -usually on Ser, Thr, Tyr AA (all w/ OH groups, no charge) -specificity from AA next to target -phos'ation changes pro. charge ->form more H bonds -favorable free energy ->conform. changes, Enzyme Regulation Allosteric enzymes Phos'ates Ser/Thr residues Contain 2 cata/2 reg subunits Cata active site -inhibited by pseudo substrate Ala, not Ser in reg. subunit cAMP dissociates subunits, Phosphorylation by kinases X-OH+ATP->X-OPO3+ADP -usually on Ser, Thr, Tyr AA (all w/ OH groups, no charge) -specificity from AA next to target -phos'ation changes pro. charge ->form more H bonds -favorable free energy ->conform. changes PKA Epinephrine-> -G-protein, ad. cyclase, cAMP ->PKA->Phos. Kinase-> Glycogen Phos'ase a(active) -break down mm. glycogen ->to make gluose-P ->to make ATP -AMP-allosteric activator -or activated by phos. kinase -inhibited by glucose, ATP -contains CAM subunit, O2 usage highest in mito. -mostly to make ATP -end product of fuel metabolism most ATP used to make protein -then for Na/K ATPase, Ca ATPase Marathon Runner uses 17molATP/period (period=25min run) 17mol*600g ATP/mol=10kg ATP 10kg ATP*12 periods=120kg ATP consumed cells w/ 10mM ATP*20L tissue*600g/mol =120g ATP -continually broken down, remade, Redox rxns E'=Eo'+(2.3RT/nF)log(ox/reduc) Eo'-standard reducing potential Eo'(reduced)-Eo'(oxidized)=Eo' -tendency of one substance to ox. another -strong reducers-(-)reduc. potentials -strong oxidizers-(+)reduc potentials ΔG°'=-nFEo' n=#e- transferred F=23.06kcal/Vmol, Phosphorylation by kinases X-OH+ATP->X-OPO3+ADP -usually on Ser, Thr, Tyr AA (all w/ OH groups, no charge) -specificity from AA next to target -phos'ation changes pro. charge ->form more H bonds -favorable free energy ->conform. changes PKA Phos'ates Ser/Thr residues Contain 2 cata/2 reg subunits Cata active site -inhibited by pseudo substrate Ala, not Ser in reg. subunit cAMP dissociates subunits, Std. Free Energy ΔG°=-2.3RT*log(Keq) ~-1.4logKeq reactants, products []=1M low Keq, ΔG°ɬ high Keq, ΔG°ɘ More accurate ΔG° ΔG°'->std for bio. systems ->pH=7 ΔG°->pH=0 more neg ΔG°->higher E, more favorable, Bioenergetics Coupled rxns favorable ΔG° coupled w/ unfav. ΔG° sum ΔG°s ex. Thiokinase, Enzyme Regulation Allosteric enzymes More than 1 cata, reg site -sigmoidal V vs. [S] usually (unreg'd enzs are hyperbolic) reg. cmpd is dissimilar to S 2 state model-> R-low Km, high activity (activator) T-high Km, low activity (inhibitor)