the 1st unicram (4 part 2) Flashcards

1
Q

What are enzymes?

A

protein catalysts which aid in the acceleration of reactions

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2
Q

Examples of some enzyme supported reactions?

A

Hydragtion of CO2 to form carbonic acid

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3
Q

What happens during the transitionary stae of a reaction?

A

Transitionary stae has higher energy than reactants or products

Energy gets provided by the vibrational energy within a system. Molecule which has enough energy to overcome the activation energy will undergo a reaction

The more substrate molecules that reach activation energy, the fast the reaction

Enzymes reduce the activation energy of a reaction, decreasing time taken to convert reactants into products

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4
Q

What is the active site?

A

Region of the enzyme where substrate and any additional prosthetic groups bind to. Consists of many amino acid residues which help with:

Binding site amino acids (Aids in substrate orientation)
Catalytic site amino acids (Aids in breaking or forming of new bonds)

3D cleft like structure

Specicifity of the binding site is dependant on the precision of arrangement of amino acids

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5
Q

What is irreversible enzyme inhibition?

A

When an inhibitor molecule binds to the enzyme so tightly, the enzyme is made non-functional
OR
Covalent bonds permanently alter the active site of the enzyme

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6
Q

What is reversible enzyme inhibition?

A

When the inhibitor molecule can bind and unbind to the enzyme without permanent damage

Can be due to blocking of the active site or attaching to the allosteric site

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7
Q

How does irreversible inhibition work?

A

Irreversible inhibitor molecules have strong electrophilic groups, they react with nucleophiles within the structure of the enzyme

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8
Q

What are Enzyme pathways?

A

The use of multiple enzymes to complete the conversion of one compound into another

Enzyme catalysed reactions are singular chemical reaction steps

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9
Q

What are the basic strategies for metabolism?

A

Production/utilisation of ATP within the metabolic pathway

Production/utilisation of NADPH within the metabolic pathway (Major electron donor, donates electrons)

Biomolecules are constructed from several smaller building blocks

Biosynthetic and degradative pathways are almost always distinct and separate

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10
Q

How are enzyme pathways regulated?

A

Allosteric interactions
Modification of enzyme via covalent bonding
Concentration of enzyme
Compartmentalisation of enzyme pathways
Metabolic specialisation of organs

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11
Q

Allosteric interactions: Negative + Positive

A

binding negative or positive allosteric effectors to enzymes can either inhibit or activate a reaction pathway

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12
Q

Covalent modification of enzymes

A

Phosphorylation: Increases negative charge

acetylation: hide the positive charge

Prenylation: alters hydrophobicity of the enzyme

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13
Q

Metabolic specialisation of organs?

A

Different organs within complex eukaryotic organisms have a diverse range of metabolic processes which are unique for them

Organisation of enzyme pathways will increase overall efficiency

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