1/14
Flashcards on Regulation of Glycolysis
Name | Mastery | Learn | Test | Matching | Spaced |
---|
No study sessions yet.
Hexokinase
Catalyzes the irreversible conversion of glucose to glucose 6-phosphate (G6P).
Phosphofructokinase-1 (PFK-1)
Catalyzes the irreversible phosphorylation of fructose 6-phosphate (F6P) to fructose 1,6-phosphate (F1,6-P).
Pyruvate Kinase
Catalyzes the irreversible conversion of phosphoenolpyruvate (PEP) to pyruvate.
Phosphoglycerate Kinase
Catalyzes the conversion of 1,3-bisphosphoglycerate (1,3-BPG) to 3-phosphoglycerate (3-PG), yielding 2 ATP per glucose.
Glyceraldehyde 3-phosphate dehydrogenase
Catalyzes the conversion of glyceraldehyde 3-phosphate dehydrogenase, yielding 2 NADH per glucose.
Allosteric site
Site other than the active site which can control the overall three-dimensional shape of the enzyme, resulting in activation or inhibition.
Insulin
Released from pancreatic beta cells when glucose levels are high; activates hexokinase and glucokinase, stimulating glycolysis and inhibiting gluconeogenesis.
Glucagon
Released from pancreatic alpha cells when glucose levels are low; inhibits hexokinase and glucokinase, stimulating glycolysis and inhibiting gluconeogenesis.
Citrate
Krebs Cycle intermediate; ↑ citrate = ↑ Krebs cycle activity = ↑ NADH, FADH2 = ↑ ATP = ↑ energy supply
Fructose 2,6-bisphosphate (F2,6-BP)
Most powerful regulator of PFK-1. When its concentration decreases, it also stimulates fructose 1,6-bisphosphatase which eventually converts that to glucose.
Adenosine diphosphate (ADP)
ATP is broken down into ADP and inorganic phosphate by hydrolysis.
Phosphofructokinase-2 (PFK-2) / Fructose 2,6-bisphosphatase (F2,6-BPase)
An enzyme complex with two different types of domains that can be allosterically and hormonally regulated.
Feed forward reaction
Metabolite produced early in the pathway activates an enzyme that catalyze a reaction further down the pathway.
Long-Chain Fatty Acyl CoA (LCFA)
Undergoes beta oxidation producing acetyl CoA.
Arsenate
Competes with organic phosphate as a substrate for G3-PDH, forming a complex that spontaneously hydrolyzes to form 3-phosphoglycerate, bypassing the synthesis of and phosphate transfer from 1,3-BPG.