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Handout 4 - Enzymes as Drug Targets

by: Evan Roberts

Handout 4 - Enzymes as Drug Targets CH 405/505

Marketplace > University of Alabama - Tuscaloosa > Chemistry > CH 405/505 > Handout 4 Enzymes as Drug Targets
Evan Roberts
GPA 3.57
Medicinal Chemistry
Timothy Snowden

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About this Document

Filled-in handout on the structure-function relationship of enzymes, as well as a basic overview of enzyme inhibition and Michaelis-Menten kinetics.
Medicinal Chemistry
Timothy Snowden
One Day of Notes
25 ?




Popular in Medicinal Chemistry

Popular in Chemistry

This 12 page One Day of Notes was uploaded by Evan Roberts on Friday January 23, 2015. The One Day of Notes belongs to CH 405/505 at University of Alabama - Tuscaloosa taught by Timothy Snowden in Spring2015. Since its upload, it has received 97 views. For similar materials see Medicinal Chemistry in Chemistry at University of Alabama - Tuscaloosa.

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Date Created: 01/23/15
Patrick An Introduction to Medicinal Chemistry 5e Enzyme Fuml ntals Chemical reactions at physiological pH and temperature are too slow to support life y39 quotif Ratelimiting r Reactlon Enzyme I Iiquot 1 1 Binding Commonly multiple chemical steps 2 Te Active Site Hydrophobic hollow or cleft on the enzyme surface 0 Accepts reactants substrates and cofactors Contains amino acids which bind reactants substrates and cofactors catalyse the reaction Active site Active Slte Substrate Biudm Substrate 39 Induced t Notes 0 Active site is nearly the correct shape for the substrate 0 Binding alters the shape of the enzyme chm 0 Binding also fgmbmaes 39i39mn39fs xj39gsu 3 in the substrate 0 Substrate becomes for reaction Bonding forces 0 Ionic Hbonding 0 van der Waals Emailla Binding of pyruvie acid LDH Possible interactions HBond van der Waals I nailing forces Induced t Active site alters shape to maximise intermolecular bonding lgllmuniisii iianngi nggIlI39l lri39iliilili IlilIlliiEiiiiiEEAEHIEE EIHIIIIllil llllIlllili ii i i l 39 m IliIiililiiliiquotii ll lllii iiliillll Induced t Intermolecular bonds not optimum Intermolecular bond lengths optimised length for maximum bonding Susceptible bonds in substrate strained Susceptible bonds in substrate more easily broken ms SWIVIH or Cl slebili L WEHM Catalysis mechanisms 0 Histidine s9 sz JPN h Nonionised lonised Acts as a basic catalyst Acts as an acid catalyst proton 39sink39 proton source LSerine LCysteine 4 Catalysis w n chino 39 sin acidbase amp nucleophilic catalysis C ntc r wglm sitHag ofscrinc histidime and aspartate a k 7 a 5 E FILC E iiin H1quot j Ft mm lt 1 n we I r await Catalysis chanisms fur EEEMIJK inf c 7 PrutalianHH Prnteln C I 1y ITH l r ps i n x MEchauiism Em thymequot 1 9 ll 7 ll O J I E NH Pr t lm Pratem 4 Catalysis mechanisms Mechanism fur fhym trypsin III 9 cm Fmtelm 7 GEEHH Pmt in C I 1y I nolrry39 psi I ii Menhanism far thymutwpsin Protein Catalysis lmnisms Machinism far chyma quot Pmtain 7 j 7 Catalysis mechanisms Mechanism fur thymotijrpsin 7 H Protein 26 Case Si udkL I S l aHnS Cf39 i Catalysis L Vquot M Mechanism for e hi39jmutrypsin O O OH Protein ES 2 ES EP EP Notes 0 Binding interactions must be strong enough to hold the substrate suf ciently long for the reaction to occur 0 Interactions with product must be 7 Weak enough to allow it to depart quickly 0 Designing molecules with stronger binding interactions results in enzyme 139 Hawker which block the active site Regulation oiquot Red woe a 5 X Transport proteins or upstream enzymes MUCL LE 77 H E lt5 H c m Repress gene expression mRNA or translation 0quot EMT ff 01 SON 6 a U 4quot 5 Deactlvate Enzyme 3 8 l allos39ccrf C inhibition code t eg kinase inhibition cell messenger binding inhibition indirect quot mes Allosteric Inhibition Active site Am Sit unrec lsable Induced t A v 2 binding site Allosteric Inhibitor or activator collectively called modulators Inhibitor binds mlw to an allosteric binding site 0 Induced fit alters the shape of the Mullquot 950 E g enzyme at r 0 Active site is distorted and is not recognised by the substrate 3 mbla w 0 Increasing substrate concentration not reverse inhibition Allosteric inhibitor is not similar in structure to the substrate Regulation of Inhibition Biosynthetic pathway i I 999 quot391 P f P 39 P Inhibition YouBbcQL control Notes Allosteric regulation is most common in multienzyme pathways 0 Enzyme is controlled by the concentration of the nal product of the pathway andor a product from a Sapm lt up 441 A Other products from the same pathway do not inhibit enzyme Because allosteric binding is reversible when P decreases the enzyme activity dunL715 assuming a feedback product from a different pathway is not involved ulation of Enzymes Phospho Control External signals can regulate the activity of enzymes eg neurotransmitters or hormones Second messenger produced initiates a signal cascade which activates enzymes called protein kingses 0 Protein kinases powwow a target enzymes at Y S or T to activate or deactivate them roln phminonigs dephosphorylate producing opposite effect I I Surface ccll finiep39inr 1 Hormone eg epinephrine insulin glucagon First messenger Miehael s Mente Graphical of KM Rate of i quot ff39 fr39 ratemax Vmax reaction 39 kmtughot ratemax u I E KM 51 Product I Ratelimiting Fast I Reatctie I Under saturation kineticsquot kcat k3 assuming k3 is much lower than k1 or k2 KM KD lg Ifwlgzytk S 05Vmaxassuming no afxosmt control Typically1 Ojitoji171fifor most enzyme substrates Indicates how we a substrate binds lower is better Compound with largest kcatKM speci city constant is considered the best substrate for a given enzyme Kinetics Lineweavere u rke Plats 1Vo Slope KMVmax Intercept 1KM Intercept 1 me o 1S Figure 012 lluhemlum Seventh Idlclen O 2012 W H freemen end Company


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