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Th1L07 Regulation of enzyme activity
Descripción
(Theme 1 | Cells and organelles) Medicine Y1 Mapa Mental sobre Th1L07 Regulation of enzyme activity, creado por Emma Allde el 17/08/2016.
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medicine y1
theme 1 | cells and organelles
Mapa Mental por
Emma Allde
, actualizado hace más de 1 año
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Creado por
Emma Allde
hace casi 8 años
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Resumen del Recurso
Th1L07 Regulation of enzyme activity
Allosteric regulation
regulation of a protein by binding an effector molecule at a site other than the protein's active site
that site is the allosteric site
allow effectors to bind to the protein, often resulting in a conformational change involving protein dynamics
Sigmoid curve (compared to hyperbolic curve of M-M kinetics)
Allosteric activator
Opens up active site, making it more open to substrate
more or less effective active site
Negative allosteric effectors
Eg. ATP and citrate on phosphofructokinase (metabolism)
ATP can act as positive regulator during glycolysis if there is not enough ATP and citrate
Positive allosteric effectors
Eg. - "phosphoenolpyruvate (PEP) and fructose 1,6 bis phosphate on pyruvate kinase
PFK acts as a positive allosteric regulator of phosphenyolpyruvate to pyruvate (a later step in glycolysis); good example of co-ordinated regulation
Pharmacological altering of enzyme activity
Covalent modification by other enzymes
Most common form is the addition or removal of phosphate from Ser, Thr, Tyr, His residues
Dephosphorylation of serine 14
by phosphorylase phosphatase
Glycogen synthase kinase 3
phosphorylates at several serine resides; inactivates the enzyme entirely
Glucose metabolism
Coordinated regulation of synthesis and breakdown of glycogen via adrenaline and glucagon
Shows how protein phosphorylation may be increasing or decreasing activity of even catalysis of a different reaction
Phosphorylation (regulation of glucose metabolism)
Single cascade system
Increases activity of glycogen phosphorylase, which is responsible for degrading glycogen
occurs by phosphorylase kinase serine 14 and requires ATP; ALSO reduces activity of glycogen synthase (synthesises glycogen)
Other
Adenylylation or AMPylation (Tyr residues, ATP to PPi)
Uridylylation (Tyr residues, UTP to PPi)"
Induction or repression of enzyme synthesis
e.g. High blood glucose levels lead to an increase in insulin production
Insulin increases rate of synthesis of key enzymes involved in glucose metabolism
Glucokinase, phosphofructokinase, pyruvate kinase
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