Class Note for CHEM 490 at UMass(13)
Class Note for CHEM 490 at UMass(13)
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This 20 page Class Notes was uploaded by an elite notetaker on Friday February 6, 2015. The Class Notes belongs to a course at University of Massachusetts taught by a professor in Fall. Since its upload, it has received 17 views.
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Date Created: 02/06/15
Protein Function catalysis Ch 89 Fri 22709 Enzymes 2 catalysts enhance rates no equilibrium Binding general chemistry specific 0 Enzymes land substrate transtian state a iiilichaglsilileznte n kinetic QQlJl iiiQ WSCUWVES 0 Inhibitors How Binding effects Proximity Transition state stabilization Chemical effects General acidbase Covalent catalysis Chymotrypsin example deducing mechanisms bol k Enzyme regulation Ch 10 unnumherad gure pg ma 51mm Mwa 7 spum cu o 5 CNquot2 Hz ch o H2C 0 Hzc 9 H n I n 9 x 3 0 O 2 o HCH o HCHZ H0 H2C 0 4 WNWquot 19w 439 Ala Phe Asn Ser Met Glu MWT C r32 o H2C I H o HitN H a 0 N I O NmelylLphenylnlnnine pnilrnpllenyl ester O H20 1 quot2X n C OH Hc N c H II 0 pNilropllenolu39e Figures3 Hinrhzmis 7 Six hEdi inn blot Steadystate phase K aws Burst phase Absorbance trophenol released gt 39nl Milliseconds after mixing gt WW3 Ad I p A39bs lt lt v 3 L A A 61 B o 4 0 O 0 Acylation Deacylatiul l OH x C N o c r OH H0 C R R 0 R xH ROH ester RNH2amide Enxyme AcyIenxyme Enzyme cowlava m mm W mum and mummy Ml Hiurhzmv xlly Sixm Editian r0 wu w HFmemun and comm 0 edrnl AK Ionz nu M 1 JG 5 b w km High1 N ll w quot39 A ALL R PM nef w oxyanioquot Aqlemynn hole 9 quot HMS I aquot TA M 1 2 0 n n n gaww ucnru QWMWfo l elrulmlrnl AqIenlyma iniermedinle 19 kw mar L H ro zoow HFleampmanund umple 1 Oxyanion hole rigm as sigmmrm 5m sum munw HFmemanaud mummy Scissile bond Scissile bond 1 h S 3 SIAM 226 r M3 2 g c 9 15 Ser 189 Asp 189 Chymoirypsin 39I39rypsin Scissile bond w Ala 36 3 5M 5 Lhr216 M E 225 539 Shllwflkhd39 Elusiuse Figure I I 27 Fundamemals MBiamzmislryJe zob lohnwileyampsnns Voet Voet Pratt Figure 944 Asn 155 7 7 mammary n Edikian moow HF in and mum SMNSM Asp 32 Wild type 10 ngm 916 Biathrml ry Shth mmquot munw HFleemanand Camaaxw 49quot D32A 221A 1A H64A H64A D32A mo x 3151 cat 9 gt Q l 5 quot 030M C9 392 z39 35 pH 0 Pepsin b Glucose 6phosphatase r v I gt1 INK A rL M 2b v EL I p 39 Lehninger W quotL N th 9 Enzyme regulation Ch 10 Allos reric con rrol feedback inhibi rion Isozymes Reversible covalen r modification Phosphorylo rion pro rei n ki noses Dephosphoryla rion pro rei n phospho roses Pro reoly ric oc rivo rion Zymogen or proenzyme inoc rive precursor Con rrol of enzyme Transcription or o rher s rages NH2 0C 0P0 Curlmmoyl phosphuie Figure 104 mmer51mm wanw HFleeumlund mum 0 H CH2 X H3N COO39 Aspuriuie 0 1 oc NH2H CH2 c 393 n coo NCnrbnmoyluspu uie HO OH Cy dine iripllospllule CTP ri gt gt Regulamy 139 sh R slule less active more active Favored by CTP binding Favored by substrate binding Rate of Ncarbamoylaspartate formation 10 Rate of Ncarbamoylaspartate formation gt 2mMATP 20 Aspartate mM Rstate curve Rate of Ncarbamoylaspartate formation gt Aspartate gt T state curve 10 20 Aspartate mM 04 mM CTP max 2 9 39 0 39 0 N vquot l N Pratein kinase 0 y OKy39K K KOW g a o o N HO OH Serine ATP quotweaning or Iyrnslne NM2 residue 0 2 2 s1 FT N x 5 N N H L o 0 o 6 ow NJ HO OH Pllnsphorylulad ADP protein 0 2 Protein 0 2 0 hos hatase HO 0 P P o W F H20 won F c39 d Phosphoryluled Orlhophosphule protein Pi Chymolrypsinogen inactive 1 245 Trypsin nChymoirypsm active 1 15 16 245 wChymotrypsin uChymoirypsin TWO diPePtidES active 1 1 3 1 6 146 1 49 245 A chain B chain C chain rigumuql 51mman Six m Edikilm mzaozw anaemmmm mummy INTRINSIC PATHWAY Damaged sulfate 1 Ki 39nngen Kallikrein EXTRINSIC PATHWAY FINAL COMMON PATHWAY activated by thrombin Figure was Biamzmr39stry Six m Editian mauzw Mummy Campmy
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