Question

describe in details how different types of inhibitions affect Vmax and Km values, and illustrate the changes using double-reciprocal plots.

Answer 1

- Inhibition :- ko than substrate than da substances other bend with enzyme oll E-Scomplex and decrease the cate of the elan inhibitor Types :- & Reversible. o Ieneverseble Removal of inhibitor easy موم امبابه وط نے کہا ہے binding is covalent b/w inhibitor and E ou Es complex Removal of inhibitor from medirem difficult through dilution on dialysis. ③ Un-com petitive Reversible inhibition typesa O competitive Non-competitive inhibitoes and substecate compete to bind at the same site of the enzyme. Et I preferred then crate slowed down. Model -

Many models are presented for competitive Tennibition. Model - (I Binding site & I ands different but when I binds torming E-I the conformation a S-binding site changes .sos although fite i available Scanne bind affects reale Model 5 steric factor I Model - overlapping site in E; if binds ist then saan can no longer bind. 19 Model- & No overlapping sites, stile hindrance affects the rate. 3 General conclusion. If the inhibitore binds, then the seebsteate cannot bind and the late of the elen slows. doron.

ng Mechanism for competitive inhibitions E+ I EI rts E+S - RI TR-1 2E+P. Applying SSA to [E I] and [ES] d (EI) = 0 = t; TE][I]-RiTEI]. => kilTE]- [ES]-[EI]) [I]= RiTED! > Fi (It.) - tes] - TEI])[E]:TET). » Ke (Teo] - (ES)- TE I)) [I] = [EI]- 0 Again, a tes] = 0 = R, CE] [s] * kz [ES]- R., [ES] » k, (TE]-TEs]-[ET]] [s] = (k~,+ k ₂ ) [es] => 0= @ =Ki[[Eb]-TES)-TE 1]) [1] CEIJ ki(CE). -[E<]-[ET])[<J (k_, +) [ES] Ki [I]. (kaitk) TES] - CEI] dt R. Ts] > Ki.kom. [I] [es] = [EI - 6 we are berging to expecess [ES] En teams of TE I] ; since both are coupled! From , kafleo] - Ki Km (I). [ES]-[es]) [s] = km Tes] TEo] [S]. Ahorst » TEST - Kikm [T]/ext [s]+ km

Rate = K₂ [ES]. - R₂[E ] [s] - [s] + Kekm[I]+ km 8 km Michelis menten dieiectly used here as it is a single substrate aan. Here's [I] is not the subst nate so there is no need to make it fere fecom any constant.

my competitive Inhibition : [s]+Kikm[I] + km R2 [EoJp [8]. = EST (ki km[I] +km). I K, TE JEST R₂ TE] [SI [Eo]. TEoJ ) [ED] ) [eo] e (Eol, Ceo] I lope ant YES]. [I2 cinitial cone.) [1]) [13]} [137 [I]L scope only [13] YES]

uncompetitive Inhibition : In this case inhibitore binds only with the Es complex, cannot bind with the fouce. enzyme E+SRL ES - ks, EXP. ESTI IES... I k-i Applying SSA to TEs] and [IES] & CIES) = 0 = ki [ES] (1)-K-i CIES] >> (IES) = Ki (ES] [I]. >> TIES] = ki [ES] [T]. Again, I TEs] = OFRI TE] [s] – (k~, tka) [ES]. ki ((Eo] - TES]-[IES]) [s] = (k~, the) [ES] 2. ([[o] - [ES] - RETEs] [I]) [s]. - Km Tes] =0 [Putting R-1 + 22 - K » [ES] = [eo] [S]. [s]+Kits] [I]tkm .: Rate = kz [ES] 2 R2 [ Eo] Ts] [s]+ kits] [I]+ km.

Xm ng Uncompetitive enhibition : s]+ Kits][1] + m K2 CEOJ IST + ke [I] tej katet * (ki[I]+4 km 企ET're。 RE] [Eola [E], [E], } [EO] Y [eo] Elastite potrebe Pics]

. [I ] [I][I] [I]. ] only intercept & [IJ. [I

Non - competitive Inhibition : Et I EI Ki ka EtP Ets Here; I can interact with Eqeree) and ts, unlike competitive mech. where I has no. interaction with ES... Here; Felce enzyme for I a Estes both. So [E] - (CE.] + [ES])- [ET] - CE5] = TEJ F PETJ such situation is possible only when a site f I and 5 far apart. Es does not influence binding of I but binding of I Offerts Jubstrate binding wee SSA to [es] and TEI], & TEIJ =O= ki TEJ (I J- k-i TEI]. - Ri ((Eo] - [EI]) (I] = kai TEI]. as [1] [60] - [FI] [1]- KiTEI] & TEI] = [Eo] [IE] ([I]tki) Again, & [Es=0 = R, [E] [s] - (Ray tky) [es] dt aki ((Eo] - TE I]- [ES]) [s] = (k~, the) Tes]. » there no I involved. [Eo] - TES] [E] [I] [s] - Ritka CE (Kit [IJ) / [ES] - TED] [S].- EJOTI (59 [s] +/Ratkal -

-> [ES] - [EO] [] - LEO. Г.7 Ст] с] ki * [I] Ts] tkm. >> TES] = Teo][s] Ki + [E] TSJCI)- (BOVCI] [8] (km + [s]) (Kit [IJ) & TESJ = Ki TEo] Ts] CÁ + )/ K-II) cate = K2 TES] Ikki CET [5] (km + [s]) (Kit[I]). = (km + [s]) (kit (II) Raki [E] ES]. km (kit[I]) kit[I] R₂ Kiteo] [s] kki [Eo a

mi Non-competitive Inhibitin! e = (km + ts]) (Kit[I kake (56] km(kit[I] Kit CI] k Ki [E7EsJkki LEJ Teo] CEoliy [Eola) [ [o] 3. TEO]2 ceold Lupe Into at TEoj;

[12), whori (tag) th] slope wees (1+ ]) [I Grazis x-anus intercept = حم -/km Ves]

nature Fecom nature of the graph we get an édea about type of inhibition mechanism.