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L-33_34 - at'ies CH 8 CH 30 acetoacotat‘e'i CH ~CH 0...

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Unformatted text preview: at 'ies CH: 8 CH; 30- acetoacotat‘e'i CH,- ~CH,- 0- B-hydroxybutyrate O CH ,- (f-CH, acetone 1. fl-Kelomiolgse . acetoacetyl CoA O O \\C—-S-CoA ' \\C-S—CoA §c_s—CoA l 2- l l Ii: W11: CPI; CH3 (1: W l o \, /C-CH, ’ HO— c—CH, 3. _/: ; \C—CH, ~ I W |> » g . . + CH, Wm CH, a CH; CH, CH_1 GOA-SH I I acelone I _ . COO C00 / CnS—CoA O 3-hydroxy-3-mclhyl- accloacetale glplalyl coenzymc A (I-IMG CoA) H" + NADH NADO acetoacetale 5 4. d 3 D-3-llydroxybutyralc -udro - l v e dchrdrggczlgzc 105 fatty acid oxidation LIVER fatty acids *9 acetyl CoA 6—9 acetoacetate $9 3-hydroxybutyrate ’i‘ 4\ BLOOD : I t \l, MUSCLE CO A’I'Péfi acetyl CoA acetoacetate H3-hydroxybutyrate .OR BRAIN citric acid cycle Sued-M32 Cofi Succo‘nate ace. oacd'fil C'oA 106 - ” i 'o es's a. Overall reaction of fatty acid biosynthesis l4 NADPH + 8 acetyl CoA + 7 ATP ---> palmitate (cw) + 14 NADP‘ + s CoA + 7 ADP + 7 Pi +H,o g biotin O ' CH, -S-CoA + co, + ATP --->~o.6-CH,- -S-CoA + ADP + Pi \ 5N)! CO,+ATP+ ‘ ----—> a +ADP'+Pi ,0 (CH , iaio'i'ln Cfl’fi ' ilxg’o ll Eta “he—'3 O ~o-f:-CH,-g.s-ctm ' eta-8.3 cm Mlonyl Con - Acetyl CoA carboxylase, being the first enzyme in the biosynthetic pathway, is rate limiting - It is a highly regulated - inactivated by phosphorylation (favored by glucagon) - activated by dephosphotylation (favored by insulin) ~ citrate also increases the activity allosterically c. Chain elongation occurs with fatty acid bound to a carrier protein, mm (ACP). which has a prosthetic group related to CoASH. In eucaryotes ACP is actually part of a multifunction polypeptide fatty acid synthetase. “wszszgga, ' NM .4. ............... _ “My-ivm'i‘iiiEheiiicwm o o Ciiylfi-s CoA + ACPSl-I —> crabs-mp + CoASH malonyl—CoA+ ACPSH —-.9 131 tCl? + CoASH 0 O \ 0 H,c.6-s- E19 + .O>C~CH,-&-S-ACP Malonyl ACP B-Ketoafll ACP anthems: Condensation B-Ketoacyl-ACP 11,0 6 C11, 6 S-ACP NADPH E-Ketoagxl ACP reductase Reduction CYCLE l NADP’ . D-3-Hydroxybutytyl-ACP 11¢,C- :~CH,— gus ACP B~Hydroxyacyl ACP dehydrataso1-1:):41 Dehydration h trans-N enoyl-ACP H,c-6=q. -S-ACP NADPH enoyl ACP reductasc Reduction NADP' ButyryI'ACP H,C'CH3-CH:-8-S°ACP 6 malonyl ACP CYCLE 2-7 Palmitoyl (C,.)-S-ACP 11,0 Palmime + ACP 1. Acetyl CoA + 7 malonyl CoA + 14 NADPH + 7 Hz.) palmitate + 7 co, + 14 NADP’ + 3 60A + 6 H10 2. 7Ac¢tleoA+7C0,+7ATP—) 7malony|CoA+7ADP+7Pl+71~P overall reaction is 3. 8 Acetyl CoA + 7 ATP + 14 NADPH H palmilate 4- l4 NADP' + 8 CoA + 6 H10 + 7 ADP °+ 7 P 132 WWW fatty mocnounmon t cwosom. - Acetyl CoA l ATP ADP + Pi / Citrate ——fll Citrate . i , Acetyl CoA. i xaloacetate Oxal acetate l NADH i. NAD‘ i late Pi + ADP CO, 60.. l ATP Pymvete<§|_ Pymvate NADP’ i NADPH Citmte is the carrier of acetyl gteups from the mitochondrion to the cytosot. This is ammplished by the action of W and mm. ' O o;- GoASH CH,~&-S-CoA ATP ‘ acetyl CoA + oxaloacetate fiflO- -CO," 4—9 + 4. AKIN BL , "a O,“ . curate O,’ citrate = 0 Manse M H: citrate O,” oxaloaeetate O,‘ O,‘ H -H + NADP‘ fl, Euo + NADPH + C0, + H". . ‘ H O,“ ’ malnte pyruvate Reducing equivalents (NADPH) are also provided by the dehydrogenases of the pentose phosphate shunt. 134 acid $51 Plasma membrane: Gluedse-s-P I col sis ‘NADP" 'NADPH +-n+ g y y ‘Maiata 44—» Pyruvate mar Acyl-COA ‘DHJV' Pyruvate I! Oxidation ‘/6L ‘ ‘\ K t A ‘ a one Oxaloacntate .Oxaloacama . cetyl-CoA -—’ bodlas . I TCA cycle 4—- Citrate Mltochondrlal membrane Phosphollpld Acyl carnltlne _ + Acyi carnlllno / Tfiacylglycorol \ I ACYI‘COA \ 9 Fatty acid ‘ synthase . I. I rat. 90 Q01 ‘ t l 3 BS BE F Parameter Intracellular location initial substrates thioester linkage of Intermediates Coenzymes bicarbonate dependence energy state favoring process citrate activation acyl CoA inhibition highest activity CID S S Oxidation Mitochondria fatty acyl CoA CoASH FAD. NAD‘ no high ADP no no fasting, starvation 136 Cytoplasm Acetyl CoA, Malonyl CoA Protein an (ACP) NADPH + H‘ yes high ATP .yes yes carbohydrate {ed ...
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