Week 5 - Metabolism 1 Flashcards
Describe metabolism
The complete set of catabolic and anabolic reactions that occur within living cells
Define anabolic and catabolic reactions
Anabolic = synthesises large molecules from small ones
Catabolic = breakdown f big molecules into small ones
What is the first step of sugar oxidation
Glycolysis
Describe glycolysis
10 reactions, where ATP is used in reactions 1-3. NAD is then reduced later on and in steps 7-10 ATP is generated. Net yield of 2 ATP
What do you start with and end with in glycolysis
Glucose at the start and 2 x pyruvate at the end
What is the regulatory enzyme of glycolysis and what’s is it inhibited and stimulated by
PFK
Stimulated by AMP and fructose-2,6-bisphosphate
Inhibited by ATP, low pH an citrate
Where does lactate come from
When no O2 present pyruvate accepts electrons to form lactate
Where does pyruvate go and what happens to it
Into the mitochondria where it’s decarboxylated into acetyl CoA
How do fats become Acetyl CoA
Beta oxidation
Describe how fatty acids prepare for beta oxidation
Fatty acids become fatty acyl CoA and move into mitochondria
Describe beta oxidation
Beta oxidation 4 reactions which reduces amount of carbons on fatty acyl CoA until the fatty acid is completely degraded. Forms acetyl CoA, NADH and FADH2 per cycle.
Describe the TCA cycle
Complete oxidation of C on acetyl CoA to yield 3NADH 1FADH and 1GTP
(Acetyl CoA + Oxaloacetate -> citrate -> isocitrate -> a-ketoglutarate -> succinyl CoA -> succinate -> fumarate -> malate -> oxaloacetate)
Which 2 enzymes control the TCA cycle
Isocitrate dehydrogenase and a-ketoglutarate dehydrogenase
What stimulates and inhibits isocitrate dehydrogenase
Stimulated by
ADP, NAD, Isocitrate
Inhibited by
ATP, NADH
What stimulates and inhibits a-ketoglutarate dehydrogenase
Stimulated by
ADP
Inhibited by
Succinyl CoA, ATP, NADH
Where is the major site of amino acid degradation
Liver (sometimes muscles)
Name the steps in amino acid metabolism
Amino acids -> transamination* -> deamination
- amino acids can also go back into tissue protein
Describe transamination
Amino group on a protein is transferred to a keto acid. The amino group is accepted by the first keto carbon on the keto acid
What enzyme catalyses transamination
Aminotransferases
Name the two keto acids which accept amino groups
a-ketoglutarate (forms glutamate) and oxaloacetate (forms aspartate)
What is the important reactant needed for deamination
Glutamate
Describe deamination and what is it catalysed by
Glutamate has amino group, which is removed as ammonia.
Catalysed by glutamate dehydrogenase
What is important for the urea cycle
Aspartate
Describe the urea cycle
Arginine* -> ornithine -> citrulline -> argininosuccinate* -> arginine
*aspartate added to form argininosuccinate and fumarate removed to form arginine
*H2O comes in to remove urea and form ornithine
How many intermediates can the remaining C skeletons form
7
Describe the glucose alanine cycle
Muscles use BCAAs during prolongues exercise, glutamate build up forms alanine, which is released and taken by liver to be transaminated
Describe gluconeogenesis
The formation of glucose from non carbohydrate precursors
Where does gluconeogenesis occur
Liver
Describe gluconeogenesis
The reversal of glycolysis except for three steps in order to make it energetically favourable