Exam 4 - Glycogen Metabolism Flashcards
The liver consumes glycogen to form []
Muscles consume glycogen to use [] []
- Glucose
- Right away
What type of linkage creates the linear portion of glycogen?
What type of linkage creates branch points in glycogen?
- alpha-1,4 glycosidic linkage
- Alpha-1,6 glycosidic linkage
Branching normally occurs at every [] glycosyl residue within the linear molecule…
fourth
Where are the two major sites of glycogen metabolism?
- Liver
- Muscle Cells
Glycogenolysis is….?
the breakdown of glycogen into glucose or glucose 6-phosphate
Glycogenesis is…
the synthesis of glycogen from glucose
If you create glucose from glycogen - what is the net formation of ATP?
Again - what is the net formation of ATP from normal glycolysis
- NET of 3 ATP since you only need to invest 1 ATP
- Normal glycolysis NETS you 2 ATP.
What are the 2 enzymes used in the formation of glycogen –> Glucose?
- Glycogen phosphorylase
- Phoshpglucomutase
What does glycogen phosphorylase catalyze?
- Glycogen –> Glucose 1-phosphate
- Pi is used to cleave the alpha-1,4 glycosidic linkage through phosphorolysis yielding glucose 1-phosphate
What does phosphoglucomutase catalyze?
- Glucose 1-phosphate —> Glucose 6-phosphat
- interconverst glucose 1-P and glucose 6-P
Phosphoglucomutase functions in both glycogen [] and []…..and requires the catalytic intermediate - []
- Synthesis
- degradation
- Glucose 1,6-bisphosphate
What enzyme “debranches” glycogen and what is its function?
- “technically” its a 2-step enzymatic process
- 4-alpha-d-gluconotransferase
- removes 3 gluco residues from the linear portion
- amylo-alpha-1,6-glucosidase
- Makes non-phosphorylated glucose
What is the first step of Glycogen anabolism?
- Making glucose 6-phosphate from glucose
- hexokinase
What enzyme interconverts G-6-P and G-1-P for glycogen anabolism?
- Phosphoglucomutase
What enzyme uses glucose 1-phosphate and UTP to form UDP-glucose and PPi?
Glucose 1-phosphate uridylyltransferase
What is the building block for glycogen production?
UDP-glucose
What does Glucose 1-phosphate uridylyltransferase add to G-1-P to form the product = UDP-glucose??
- It actually adds a Uridine MONOPhospate
- There is already a phosphate on the glucose so it only had to add one to get the UDP…
What enzyme catalyzes the addition of a glucose from UDP-glucose to a glycogen molecule?
Can this enzyme function to create a new storage site for glycogen?
- Glycogen synthase
- NO
- this reaction cannot produce branches and it can only make existing glycogen bigger
What enzyme catalyzes the addition of alpha-1,6 linked groups to a linear chain?
How man glucosyl residues does this move to a new branch?
- Branching enzyme
- 1,4-alpha-glucan branching enzyme
- It moves 7 resides to a new branch point
What amino acid acts as the starting molecule for glycogen?
Tyrosine
How does Tyr become a “primed” starting molecule for glycogen?
What other molecule is required?
- Glycogenin
- This is a “self-glcosylating” molecule that adds 8 resudes of UDP-glucose to Tyrosine
- This forms the primed glycogenin molecule for more linear and branched UDP additions - through their respective means
What are the 2 targets for glycogen regulation?
What type of regulation do these experience?
- Glycogen Phosphorylase
- Glycogen Synthase
- Allosteric and Covalent Modification
Glycogen Phosphorylase Regulation
- Phosphorylation by phosphorylase kinase activates the [] []
- Phosphorylase a is the [] form of the enzyme
- Phosphorylase b is the [] form of the enzyme
- Which “enzyme” a or b is phosphorylated?
- glycogen Phosphorylase
- active
- inactive
- A is phosphorylated
Glycogen Phosphorylase Regulation
- What are the 3 effector molecules?
- What will glucagon signal to this enzyme (generically)
- What will insulin signal to this enzyme (generically)
- AMP (+) Phosphorylase b
- Glucose and ATP (-) on phosphorylase a
- Glucagon signals low blood sugar - causes glycogen phosphorylase to be more active and create glucose from glycogen
- Insulin will signal high blood sugar - it will work to repress glycogen phosphorylase activity