Enzymes (A2 Eby yma are catelysts that colalyce chemucel beoetions toking ploce wither, (hwhg orgomiinn . Th common with inovgante cotelysts, angymea : + spash “pe reaction without being Lancl up + prowile on alfrenative reaction pathwoy w ith lower activation 2hsray . Cocke eh clon Enzymes are very effective codedycts , caedephe efficiency of come enzymes Ore aa fellow: enzyme turnover numb Carbom’c anhydlrane 36 000000 catelane § 600 000 B-aimglose 1100 000] -golactosidace 12 S00 phosphoglucose isomerase | _—'/ 240 | succinate dehy brogenate 1150 Note ? ao cotelarhic actintty of enzymes 'S macsuredt 2 Logs rengyme actintyt the mumber of moles of substrate converted to product par pvhete etemovan mambin: tha peimbrr of substrate we lees reoeted por enzyme pir minute .Specificity of tyrrer Engymeo are ving Sprofic , gerrcally cectedycing only ona povticudin raackion . Tha specitic substince Cmatabolite) thet is on the enzyme strface andl is convertsct to product(s) is called a Substrate . Carbonic anhyobrass, Pore instante , 18 On enzyme 1m red blood cells that cotalyta the reaction : co, + Ho —* Ht, Carbon dioxide is the Substrate ih ths reaction because it fits onto the Surface of the enzyme - Water react with the carken devxide , but ony Whin the corbon dioxide is beuncl to the eng ye surface . In a ceblukere environment, this Sproctiocty 's absolutely essential » An engine must be able do dvhnguich ity substrate moleules from other molecules . Each aay ye Aas a spacific substrate, the Substrate berng the fegst Mole uke acted upon during tha enjyme —codalycadd reactionEnzyme are tan ctioning within the rales thet define cotaly Hic cctinty » they df fer Prom ov din org Chemical cotelysts ih sevarad ovpacts : * Enjymes are all large protech molecules + Highr reaction rates = Hae roti of engyme cotelyed practions ane offen ihoreaoad by fosters of (08 to 10? Himes compared to the uncatalyseck renetion and Ore Swerak ordlers of maghtnole greater than those of the corrsoponching chem cally cotelycad reaction + Milder conditions — CAzyme cotelyrecl racctious occu undlay relatively pal len concktiong + fampsreteee ansend 37°C, adimosphens pressure anh pH Grounel pacchrolity . + Greater ranction spacifietty — engymts re hnch mors choosy with bagarct to their substrode and products. Engyms ~codelysad ranctions ore chton, tha renckions do net prodack side. products . iS Copacty fow vaguledion ~ the cotelyhc ach whies of rang engyinea 6am be ragulednct by the concanfredioha of sxbstratie often than tht Substrate ( non — competitive indebstron)Shapoly bol senles The complicate ch Feldling of the proteth chain forrinthe teciong Strctune gives oe te ‘olafhs' ow ‘orawvens! of pracita gesmadre shape on the Stefeee of the enzyme . The precise shopes of These clefts have arotved do “racog nite’ and uta 7 place a porhicwlar Substrate molewle while it reads. The substrate —bincking site has a shape thet matches the shape of the substrate . Tha vegion is where the enzyme —cotndy tech rroction tokes plan it rs known a0 the active site of the engyme . Tha catalytic propsrtien ond specificity of om engyine ore determined by the chemical nodure of the Aimihe acicl Ro qreps located of the active site. The active site usually ocoupisa Less than 5% of Da ‘s 8 ce Orea omol involves ondy ia Gna arrhsn (3 to 12) of Amine acrela, The root of the enzyme structure finctiond 20 the Scaftfoldcng thet mantorna the shape o the actve srte.The_lock oma heey Imodel “The praccse spaccticity shown by engymse Com be. et ploinad by a moclel of sys actinty ao the ‘otk onnol keg / machoncein. Enyymss catelyssd reactions by bcholing to Substrates ih & mahher Similan to how & kag CHhe subrhrate) fits into a ee — active site), | é&: = @-(& | BQ ernment —> om pds eryme substrate = E+s = lock key na The Jock omol kay’ mechani em Locks ancl kegs ore complementary shuctires oncl thes wold odes explain enzyme spacitreity . Only one gubstrate will fit into the active tite 4 the m3 yin , just 20 ony one keg Fits a lock, Tha sub strode murt have the correct chope onc size to fit Ha active site & the enzyme . Tt must olac hove the Recesaany Ponctrotet groups to Forin weak bonels with the Ahuhe awe sitle-checta linthy the active site . 5Low sparple , when the substrete moleule fits into the achive site: «fa nen-pelor port of the substrate molecte i's next to hor-polar pact of enzyme, thttractons involiatng Von cler Waals! forces is rotabheshecl , -ifa slightly posiblely chargrct pantef the substrate moles is next to a slightly negatively chargrel part of the Peng ys interactiong twaret ning depote forcre 1s Ratabdishacl , The. Sepunce of reoetions /S + “the rubstrate dfPuars to the active site «the substrate binds to the active site, Pormaing an ongymne Substrate complen. © ming ack cide ~chachs ( ancl often Small wole ites or ions) at the achive site cotalyre the resckion in thes proces curtain amine and reciduea may act as proton dohers /acapfors o- machophlea, + the products diffuas ome Prom the achive sieteExample Trypsin is a digactve enzyme whch hegolro ly se pophiles derived flom proteins in ovr food . Trypsin iS very specific ancl owly bracles pophiele bonds naxt do lysine ancl ergin‘na ragcdass in pepticles . sab ate wth ‘cH, IBYside-chsin cH 216 ghycne he : 169 aspartate The active site of Aypsin willonly bincl amine acc side-chain wheek are relatively (eng anol have a posiuely chorgecl WHa* group The. trib sms show the position of atmrne aeel rsacclaca in the polypeptide chart The pocket! ot the active sife only atlows amuike acdcl p side ~chains 4 Cortech size and charge to enter. The — WH" group , which Porima when ths side char Of lysine Cor arginine) accepts @ proton com Fovin week bonds with Fhe aspartate rearlue ot the active side.The vat of the pocket is lero vs ith neor—polan Bini acck pegileroe These form weok jrdermoleclan attrachions with ths hybrocarbon part ca the lysine Cow argitihe) Side-chathe - juhen the kysike bende to the active sife , other greps ere brought op which cotmlyse the boncl— breaking reoctron . The products then df fuse aangReaction Ktheriva involving eng y ine As homognems cotelyst, omyynes fumction by prowling an altrrnotive raoctien pothwuog thot requir @ lowe Ealactvetion tren) Thus more moletukan interactions posters oufficent energy to produce products . The Following energy profile deagyann shows the formotion Of tha enjyine —Sabsteate, comple reduces the Cheng ragucirenbat for the reaction to procorcl , enthalpy progress of reaction cnegy profile for engyine ~codelysad andl non-cadelysuel reaction , The overodh reaction between ongyine onol its substrote Com be repregentecl by tha $otlowing egrotion + ENZYME + SUBSTRATE == ENZYME-SUBSTRATE —> ENZYME + (lock) (key) (key in lock) PRoDUcTsE-S complexes ave often almost 20 stable as the Seperated enzyme + Substrate, because $ the extra bowsking thet binds the wbstrate to the achive site. The first stage of the reaction i$ revsysible , Since the Ea for the dissociation of the E-S complex back to E+ § is obut the same in sizeto thot Of the breckdown of E-S into E+P. Tr Some cose, the second stage iS also reversible moking the whole engyme catelysecl proces capable $ procencling ih ecthen dévaction dapencling on the cell's metabo lic regina ments . Once the products have boom forinact , they Leave the active site of The imgyme. The engyme is then Pree to combihe with & Rows Substrate meleode . Like inorgance codalysts , em3ymes ore net uosel, up 7h the reaction thes cododyse so they Con be ged a gach and agatn ,Exscecse | Explain the terms: 1) active site i) lock anck kay mechani Workeinas i) The substrate -bindling site on the Surface of the erg yme thot matches the shape of the substrate . The tazyin -cotaly cod reaction tukes place in this region . 11) The substrate 1s complementing in shape 40 the active site of the sa3yie Tt binds tothe enzyme speccBically becouse of the matth ih Shape ane aloo matching of the positions of polar ancl hon-=pelar ragiona of the substrate amet He active site distribution of charge), The substrate is seve 4p be dike a keog in the lovk, with the active site of the sm3yne being the lockExsrose 2 Chaymmedrypsin is an eng yma that cakelyses the hagebrdlysis of propticte Chalna haxt to the amie aceck tyrosine « substrate wth tyrosine A tyrosing. residue bouncl tha active site of chymobypsin ) What Peacerea of the active site help to bine tyrosine? i) The stuctene of an alancne site-charn is Show below ———~ < Pelypephide, back bors. CH, of subetrote Suggut why the alanine residue dow net bind fo the chymotrypsin active cite «lorkcng s i) Hydrogen bonding betwen the ~OH of the tyrosine and the —OH at the bottom of pockt of the active site. Tha smal glycine side chaing oh the proten allow the large tyrosine molecules to Fit inte the active Site where it alse Ashel by von dom Waals! forces. ii) Tha, -CHy group on the alancne side-chain is qucte small, so Thdow ht get hear trgh te the polypeptide charn at The active site to be stabilised by vom der Waals! Forcea . H+ dou nt Ft for ervsah jnto the pocket to be stabolkised by side chacns of omy other aluils Acc residues .Exsreise 3 Draw an tnrgy profile diagram to chow a ‘typecal uncedalysed andh ongye—codelysad reaction On your diagram Show ! 1) the activation energy for the cortoly cart and Uncatedyced react’on i) the enzyme , substrate onck product and tha engyme —Srbstrate complex. Werlengs progrtes of reackon file Enzyme E-S 3 Ensyme = Subst complex Substrate Pt Procluct