Enctors affecting engyme activity (A>) The catalyhe actinty of engyne is dependent on these Velotively weok, but Anghly significant interactions thot gre vise to the thersa— dimemtonal tertiang Structure of The protech , The interactivny betwam the sibstrate ond the engyme alec jrvelvet the same Kind of men— covalent fittractiong . Ehgyme functions bard on recognition ancl molecular Mets Evin subtle change in pH or temparectine con modkfy tha jrderactionn jhvelurct jh moleclon shape aunrcl recogmton p reouldeting 1h Om sngyiee working lower thon maximum 2ffr Comey « Interactions with other chamical substances thet Coma irreversible. changes ih structure Com ada rasult ih loss of the correct structure anol the deatuccion of engyme achiinty Arar n. an denoduration .The effecd of tebprredture The +f fect of Feempre echo, oh Ang yne achinty Ps tha otcome of Severed dffrrtnt fretors : «tha spasch of the mole cles the Eo of the codelyed remctron + tha therinel sto Cty of eng yas onol the Substrate. At low temper sctiran (Coreuncl 0°C), the rate of most enzyme - catalysed reoctions is very low. The molecules involved in the reoction have low kinetic eosray » They do net collide Pegusrtly ond oven whan they do, tha molacules do bet possess the hninimuin energy (Ee) raguinad for rnection te oscer. Tha inyyme 18 sec to be deachivertedd by lew taryorr eto : Incraseing Temperature ihoraaste the rete of nage acti ty sihte the molecales invelved have gy seten kecnetic energy : Betwon O° C omel approx iimately 40, the rate of engyiee activity Theraesss for veces hs Similar to ny other chabical reactions 5+ The moles are mowing mara qucetly, tneracaiing the fra punneg +t coll Sion + A greater proportion of the colksions involve mmoleeales with ensrpy graaton thon Ea for the Cotaly sek reaction , Enzyme actnity o 1 2 863 4 SOO Temperature /*C a profile of engyine achinty with temprcativg For most engymss, Ha rate of reaction ttovts to decvange above 40°C . Increased therinal mebion of the Potypephile. chen is Causing disruption of the forces mairtething the shape Of the an3yine, moleckee . The enzyme molecales ara progrusively denctoract, causing the shape of the achive site te change . Above 65°C, the enzymes from most organisms Bort completely denture by Avot .The effect pl affects enzyme actiurty . Extrema of pH (high acccity ov okkabiiity) denature protecna by oles rupting the precise 3-D arrangsmunt of the protecn chatna. Lew pH protonates - Coon side chain amd high pH deprotonatia —NH3* side —chasn . Thay deasrugts fom bonolo that Aelp Po manta py the tertiary ctuccers . Small changss arvunl rentrod pt con affect the Jonisatton of Abiko accel s/cle-~ chains ih the active site of the sngyme ancl somtimes the tabstrote if sth @/ ‘COOH q NHS” at Ge an active site piichengs con affect the ionization of "THahanqun can offek tha tonttedlion © pordiadin Bmtha Ochs cad reaitnns ot the active sit) -If angyme act ity dapende on whether particular amibe acid residues at the active Site being chow gael, then a shft a just one pH unit Co ten -Pdd charge in Ht jon concentration) Can change the enzyme actinty significantly . Most enzymes are. active over a Pacrly herew pit ronga The optitoum pH fo mest m3y meta that Work within cell 7s hear pH 7. Mang enzymes which fumchion ovtsidle cetle, such ao the. degsative enzymeo ih the Stomach onl inteatings, have optimum pls which reflect the pH of the medium in which Thay work Eck ensyms thas its own distinct optimus H: A pepsin amylase trypsin | ‘Wtieaiiiiiiienglieiiiaaaaaaaie™ curves shouiug pH optina for soma digutive enzymes* Pepsin haydrrolyses protecia to pephidas in the vers acidic conddrons of the stomach , is Armylase, hydrelyses Stach to a mixtune of glocose and maltose in the slightly alkaline conditions producact by the saliva in the mouth. + Trypsin hydrolyseo peptides to amine acctla i the mildly atkelina conditions of the stall iteatine .Exera'se | Q. Sketch a graph to show how actinty fa Aypicol enjyme Vanite ith trmparcitone 8. By ueing the graph drawn, explain in tertva of Fla kinetic Thanty ancl the affect of tamprcature Oh en3 yee shucture . orking s a Enayme actity Hamppoc tore] The enzyme activity double For wing inéceean of 10°C fom OC fe orn HePC Ergym ak wily proba ot ohot Lo°C then Shorty dacktna .8. Bilow Ho°C, enzyme achinty inereacey with Finprrct vere jn a Similar fashion to inergant® reachons The reatards are colliding with more ehergy , Se more reactants possess the activedion ensray and ture ace more succuatl collisions, Collisions cccun with grantor Fregueney on the engyme surtrce Above 40°C, the inersased vibration of the petypaptite chain desropts jeter mole oko bonding Chyerogin bonds, von ober Waale! Porter, ete.) which maiwtacha the Parting sductire in place The tactiony shuctere begcns to attr, Thea changing the Shape of The achive site So that fh cont catelys is cahnet occ At temperecturs hegher Han G0°C, th pelypaptile Chace Unfells Onol the eng yme becomes denoturedExsrecsz 2 Glitamote tRNA ligase rs a typeced engyne found in the caytop learn of the cell. Tt has @ pit optimum of pl G-7- Sketch a graph do show a pH/ingyme achinty clrve Por ths eng yine Workings ergy ach ay 2a ge FG 7 wy pH The cucve with maxiimin engymre achinity af pH G7 oncl Corveny off at ether side .Exerese3 Look ot the shape of the pH [ach wy curve for pepsin. de ai Peps amylase typtin Ene acivty \ pH The ach ty oa pepsin de pence on two mpertic acih resides at its active site. Ona of these (5 lomisacl, the other 1 rst Use thes information to explacn the pH actinty curve of pepsin.Workings The pH cueve shows an optimum enzyme oohivity ot pH 2 and decrease gucckly unt loss of enzyme achwty on ecthen cicte . The two aeparhe acd rinclass Coulel be iomsed (- coor ) or umeonised (-CooH). At the optimnuna pH jens is jomisad aml the other is net: Ais the pH clecrrases below pH 2, the iomsad group beeomia prorated , —Coo™ +Ht —» —CooH cmck togyma achuaty is lost . As the pH increas above pil 2, the — Cool grap become deprotenatec ancl enzyme achinty redacia (Note +. TAH presenta of cofscters ov other aluihe acick raavclae Com aly to \pretect' the fonisect Form of — C007 rep at such afew pH.)