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Regulatory Strategies
Allosteric Control
Multiple forms of Enzymes
Reversible covalent modifications
Proteolytic Activation
Control of the amount of protein present
Multiple Forms of Enzymes: Phosphoprotein Proteases 2A (PP2A)
Catalytic subunit has 2 Mg2+ ions on its active site
These are near the substrate recognition site
PDB ID 2NNP is the regullatory subunit
Microcystin-LR is a specific inhibitor of PP2A
PP2A recognises several target proteins, its specificity is provided by a regulatory subunit
Different subunits can fit with the scaffold unit to create unique substrate-binding sites
Control the Amount of Protein Present: PEP Carboxykinase Promoter Region
FOXO1 (transcription factor): Degraded under Insulin Receptor Activation thus reducing levels of PEP carboxykinase
CREB (transcription factor): Activated by cAMP pathway which happens when glucagon is releases
PEP Carboxykinase involved in gluconeogenesis
Control the Amount of Protein Present: Glycogen Synthesis and Degradation
Involves glycogen synthase and glycogen phosphorylase
Amount of substrates is regulated
Whole process is tightly regulated via:
-Use of different enzymes in both pathways
-Insulin dephosphorylating glycogen phosphorylase and glycogen synthase
-Glycagon or adrenaline phosphorylates them
Allosteric Regulation: Glycogen Phosphorylase
Glucose, Glucose-6-P
AMP
Insulin dephosphorylates Phosphorylase a
Double regulation both hormonally and allosterically
Allosteric Regulation: Glycogen Synthase Kinase 3
Active when dephosphorylated
Insulin increase glycogen synthase activity by encouraging dehosphorylation and inhibiting phosphorylation
Glucagon inhibits
Glucose and Glucose-6-phosphate increase
Phosphorylation happens at Serine residues by GSK3
Allosteric Regulation: FA Oxidation and Synthesis
When biosynthesis is active oxidation is inhibited via:
-Action of malonyl CoA over carnitine acyl transferase I
-Action of PPAR's
-Role of Hormones
-Action of palmitoyl CoA
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