Topic 8.1: Metabolism Flashcards Preview

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Flashcards in Topic 8.1: Metabolism Deck (21)
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Definition of metabolism

Web of all the enzyme-catalysed reactions in a cell


Metabolic pathways

Consist of chains and cycles of enzyme-catalysed reactions


Example of chains of enzyme catalyzed reactions



Example of cycle of enzyme catalyzed reactions

Krebs cycle
Calvin cycle


Definition of activation energy

Required amount of energy for a chemical reaction to proceed


How do enzymes speed up the rate of a biochemical reaction?

a) Lowering the activation energy
b) Stressing and destabilising the bonds in the substrate


Types of enzymatic reactions

a) Exergonic (Release of energy to the environment)
b) Endergonic (Absorbance of energy from the environment)


Definition of enzyme inhibitor

Molecule that disrupts the normal reaction pathway between an enzyme and a substrate


Normal enzyme reaction (3)

a) A substrate binds to an enzyme
b) The active site undergoes a conformational change to optimally interact with the substrate
c) Substrate is converted into product at an accelerated rate


Competitive inhibition (2)

a) Molecule, other than substrate, blocking the active site, preventing substrate from binding to it.
b) Its effects can be reduced by increasing substrate concentration.


Noncompetitive inhibition (2)

a) Molecule binding to an allosteric site, causing a conformational change in the active site and substrate cannot bind to it
b) Its effects cannot be mitigated by increasing substrate concentration.


Example of competitive inhibition

a) Treatment of influenza (Relenza)
b) Relenza competitively binds to the neuraminidase active site and prevents the cleavage of the protein4


Example of noncompetitive inhibition

a) Cyanide is a poison which prevents ATP production via aerobic respiration, leading to eventual death
b) By changing the shape of the active site, cytochrome oxidase can no longer pass electrons to the final acceptor (oxygen)


Definition of end-product inhibition

Negative feedback by which metabolic pathways can be controlled


Process of end-product inhibition

a) The final product in a series of reactions inhibits an enzyme from an earlier step in the sequence
b) The product binds to an allosteric site and temporarily inactivates the enzyme


Purpose of end-product inhibition

Ensure levels of an essential product are always tightly regulated


End-product inhibition of the pathway that converts threonine to isoleucine

a) Isoleucine may be synthesised from threonine in a five-step reaction pathway
b) First, threonine is converted into an intermediate compound by an enzyme.
c) Isoleucine can bind to an allosteric site on this enzyme and function as a non-competitive inhibitor


Competitive inhibition and maximum rate of enzyme activity

It can still be achieved by increasing substrate concentration


Noncompetitive inhibition and maximum rate of enzyme activity

The maximum rate of enzyme activity is reduced although substrate concentrations increase


Lock and Key Model

a) Active site complements the substrate precisely
b) Explains specificity


Induced Fit Model

a) Active site undergo conformational change when exposed to a substrate to improve binding.
b) Explains broad specificity and catalysis