Lecture 21 Pyruvate Dehydrogenase Complex-BW

Co2 even though reducing is not part of the

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Unformatted text preview: whenever you have an oxidiation you have a reduced. - loss of CO2 - the product generated - Acetly CoA - imporatnt becuase thisoester bond (high erngy) and we capture electons as NADH- this reaction occurs n matrix of mitchondira - NADH is where it needs to be to transfer to electron transport chain. 4/6/13 MCB 2000 Lecture 21 Two enzyme regualted by enrgy charge (PFK1 and pryuvate kinase) - Pryuvate Enzyme Complex - also regulated by energy charge - when ATP levels high - inhibit PDC. enzyme regulating allosterically and hormonally. - in addition to ATP - feeback inhibited by both of products. liver wll being to oxiize fatty acid for enery will not use glucose will need to make glucose. will have high NADH and high acetyl CoA. molecuels coming from fatty acid oxidiation.n to take pryvuate back to gluose. Regulation of PDC: Allosteric PDC less active PDC more active Low enrgy charge PDC more active. need to sytnthesize more ATP and pryvuate dehydrogenase c omplex - enter TCA cycle genreate more ATP the allosteric r egulation feedback inhibted by product. the enzyme product is not active with high enery charge more active when y ou need to s ynthesize ATP. and it will be activated by s ubstrate (NAD+ and pryuvate). 4/6/13 MCB 2000 Lecture 21 Fasted state: low gluocagon ratio - glucagon singalling perdominates - glucagaon signalling activates a specfi ci kinase. enzyme that regualtes a c omplex - polypetide chain - catalyic enzyme and regualtor enzyme - glucagon signalling will trigger the activation of pryuvate kinase. that kinase will also be activated by NAD and acetyl CoA - same molesulces that inhibit PDC - kinase becomes activated - teh phsorphoalyation that the enzyme remains inactive. - small molecuels like acteyl CoA - conventration can fl uate. - need a signal to remove phsophate. Regulation of PDC: Hormonal & Allosteric I/G Pyruvate ADP inhibit NADH activate Acetyl CoA I/G I/G activate [Calcium] 4/6/13 I/G Pryuvate will remain inactive is phosphylated state until level of insulin and glucaon someting. insulin s ingalling will activate a phosphate and now have an active complex. pryuvate kinase - phosophate low in liver - activated. less actie when insulin glucagon ratio is LOW. pryuvate kinase when insulin glucagon ratio high - fed state - dephosphoylatd and resumes normall activaity. - regulated allosterically and hormonally. major organ that responses clearly - liver. muscle doesn't response to glucagon - as long as it wants - wont be inhibted. as long as glucose is avilable. MCB 2000 Lecture 21...
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This note was uploaded on 09/17/2013 for the course MCB 2610 / 200 taught by Professor Feldman during the Fall '12 term at UConn.

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