OverviewLecture

OverviewLecture - / Stage 1 Glucos- ATP Hexoldrlase ADP...

Info iconThis preview shows pages 1–7. Sign up to view the full content.

View Full Document Right Arrow Icon
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Background image of page 2
Background image of page 3

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Background image of page 4
Background image of page 5

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
Background image of page 6
Background image of page 7
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: / Stage 1 Glucos- ATP Hexoldrlase ADP Gluten 6-phosphm Phosphoglucose“ CHZDH isomerase Fructose 6-phnsphato "0 ATP 0” Phosphofmctaklnase Ho ADP Payne-ht D campus!- Fruclon 1,6-blsphosphata Ho H OH Ald Ia 'I'rlose phosphate 0 n "x éo meyacltOnl fl. GUWlldihYdi f phosphah 3-phosphah "—T—m“ <CH’0" (HzflPCIJZ' D= (H10P03 ' + Stage 2 Glyceraidehyde Pi' HAD 3-phosphate o dehydrogenase ' "RD" 2'fil,PO~.c4.$" 1,3-Bisphosphoglytlrah H DH ADP _ Phosphoglycerate < CH2°P°3' kiflase ATP {Rail}! r 3-Phosphoglycora‘lo H_c| H Phosphoglycerate ] CHzopoz" mutase ' owe-#0 2 K C 2-Phosphoglynrato H_C_OP032_ K‘ imam Enolase H20 0 r ' : m 2. 04x. /CI ’ Phosphoonolpyruvau fi ADP /C X Pyruvate kinase H H ATP .t o Pyrulratl 0" \cfl | k CH3 Flgu re 1 6.2 Biochemistry, Seventh Edition © 2012 W. H. Freeman and Company coo- o | H o + E COA (lin 2 _ _ H3c/ 00C Cl—OH TOO. CH 0 0 coo- Citrate | 2 Aconitase H—‘l: H \‘c/ synthase COO“ _OOC_C_H I Citrate | T'“ 5H2 NADH + H+ C00‘ 030- NAD‘ Oxaloatetale lso‘imfle M I lsocitrate aate dehydrogenase NADH + H"' NAB... dehydrogenase _ooc + co2 T°°’ Y" HO—C—H (IZHz (ICH2 ICH2 Mnlnte I C00- coo- a-Ketoglutarule (x-Ketoglutarate NAD+ Fumarase dehydrogenase + CoA complex CoA—S \(fO NADH + H+ "20 HE /C00‘ | + (02 fi (I3H2 C Succinate coo. Succinyl CoA _ / x. 00;: H dehydrogenase I synthetase (IIHz umuruie THZ coo_ FAD”: CH2 GDP + Pi Sumnlean FAD I 67" COO- + CoA Slmimlle Figure17.15 Biochemistry, Seventh Edition © 2012 W. H. Freeman and Company Acetyl CoA COA + H20 )4, CI°°' Citrate (H2 o\c/coo_ synthase I I 'OOC—CI—OH cll'l2 CH2 (00' (L00. NADH + H+ Oxulomeluie (“rule Aconitase Malate dehydrogenase NAD“ coo- Too- H—Cl—OH Ho—T—H 'OOC—Cl—H CH CH2 l 2 C00' C00' . Mum“ lsocitrate lso‘muh Malate 'Vase synthase (200' C00' CoA cI (IZHz H/ \0 (lez Acetyl CoA Glyoxylate + H 0 C00‘ 2 Siminule Figure17.23 Biochemistry, Seventh Edition © 2012 W. H. Freeman and Company O T) O 0 II C02 I 2 e' + CoA C C C C H3c/ \‘cmx’o A Hsc/ .4 Hsc/ A.) Hsc/ \S_.C°A g ' Decarboxylation Oxidation Transfer to CoA Pyruvate Acetyl CoA Unnumbered 1 7 pSOOb Biochemistry, Seventh Edition © 2012 W. H. Freeman and Company Table 16.1 Reactions of glycolysis Step Reaction 1 Glucose + ATP —> glucose 6-phosphate + ADP + H" 2 Glucose 6-phosphate fructose 6-phosphate 3 Fructose 6-phosphate + ATP —) fructose 1.6-bisphosphate + ADP + H+ 4 Fructose 1,6-bisphosphate 1=‘ dihydroxyacetone phosphate + glyceraldehyde 3-ph 5 Dihydroxyacetone phosphate w————- glyceraldehyde 3-phosphate 6 Glyceraldehyde 3-phosphate + PI + mm+ =‘ 7 1,3-Bisphosphoglycerate + ADP 8 3-Phosphoglycerate 9 2-Phosphoglycerate —\. 1,3-bisphosphoglycerate + NAI 3-phosphoglycerate + ATP 2-phosphoglycerate phosphoenolpyruvate + H20 10 Phosphoenolpyruvate + ADP + H+ —> pyruvate + ATP AG“ in kJ mol" AG in kJ mol'1 Enzyme Reaction type (kcal moi—‘1 {kcal mol“) Hexokinase Phosphoryl transfer -16.7 [—4.0] -33.5 [—8.0] Phosphoglucose isomerase lsomerization +1.7 [+0.4] +2.5 [—0.6] Phosphofructokinase Phosphoryl transfer —14.2 [—3.4] —22.2 [—5.3] Aldolase Aldol cleavage +218 [+5.7] -1.3 [-0.3] Triose phosphate isomerase Isomerization +15 [+1 .8] +2.5 [+0.6] Glyceraldehyde 3-phosphate Phosphorylation coupled +6.3 [+1.5] —1.7[—0.4] dehydrog enase to oxidation Phosphoglycerate kinase Phosphoryl transfer —13.8 [—4.5] +1.3 [+0.3] Phosphoglycerate mutase Phosphoryl shift +4.6 [+1.1] +0.8 [+0.2] Enolase Dehydration +1.7 [+0.4] —3.3 [—0.8] Pyruvate kinase Phosphoryl transfer -31.4 [—7.5] - 16.7 [—4.0] Note: AG, the actual free—energy change, has been calculated from 06‘" and known concentrations of reactants under typical physiological conditions. Glycolysis can proceed only if the AG values of all reac- tions are negative. 111e smalls positive AG values of three of the above reactions indicate that the con— centrations of metabolites In vivo in cells undergoing glycolysis are not precisely known. Table 16.1 Biochemistry, Seventh Edition © 2012 W. H. Freeman and Company H-I- H"' ... lntermembrane H space “30.301.10.31”. "2:." a! ' WWW!!! III" . . . . Q pool Matrlx FADHZ 02 H20 Acetyl CoA Figure 18.1 7 Biochemistry, Seventh Edition © 2012 W. H. Freeman and Company I] Figure 18.33 Biochemistry, Seventh Edition © 2012 W. H. Freeman and Company ATP ATP synthase H+ Proton-motive force Matrix Intermembrane space Electron-transport chain ...
View Full Document

Page1 / 7

OverviewLecture - / Stage 1 Glucos- ATP Hexoldrlase ADP...

This preview shows document pages 1 - 7. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online