Created by gina_evans0312
about 10 years ago
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Question | Answer |
Actions- Converts Pyruvate | To Acetyl CoA |
Pryruvate Dehydrogenase- Reversible? | No, so it must be switched off in gluconeogenesis |
Structure | Multi-enzyme complex- contains E1, E2 & E3 |
E1- Pyruvate Decarboxylase | Transfers an acetyl group from pyruvate to Tyrosine Pyrophosphate (the enzyme remains bound to the TPP) |
E2- Dihydrolipoate Transacetylase (Structure) | Contains lipoate with 2 SH heads (one for the extra H from E1 product) the other for the Acetyl Group from E1 product |
E2- Function | Acetyl group on 2nd SH head is added to CoA (with the displaced H from CoA replacing it) |
E3- Dihydrolipoate Dehydrogenase (Action) | NAD+ --> NADH + H, using H bound to sulphate head group |
E3- Structure | Contains FAD group |
PD - Inhibition | Acetyl CoA: CoA ratios, & NAD+:NADH ratios |
PD Inhibition Explaination | During the oxidation of fats (i.e. starving state) NAD & CoA become scarce, so the free SH head cannot regenerate and cycle stalls |
PD- Covalent Modification (Phosphorylation Location) | On the E1 subunit by a complexed kinase |
PD- Covalent Modification (Phosphorylation Increased By) | Acetyl CoA, NADH, & ATP, as these indicate an energy rich cell |
PD- Covalent Modification (De-phosphorylation Increased By) | Mg2+, Ca2+ & insulin |
PD- Covalent Modification (De-phosphorylation Done By) | A dephosphorylase also complexed for PD |
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