enzymes Flashcards
Classify the functions of enzymes and why they are needed
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Describe the features of an enzyme active site
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Appreciate some of the key factors that contribute to rate enhancement and specificity in enzyme reactions
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Describe what is meant by competitive and non-competitive enzyme inhibition and how they may be distinguished
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•List the properties of allosteric enzymes
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Recognise that many anti-tumour and antibacterial agents act by inhibiting specific enzymes
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how enzymes achieve specificity and accelerate the speed of chemical reactions
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Evidence will be presented that some enzymes including triose phosphate isomerase have evolved to be ‘perfect’ catalysts.
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The criteria for ‘enzyme perfection’ will be described.
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Proteases. Cover the selectivity and mechanism of the serine proteases’ e.g. chymotrypsin, trypsin and elastase
They hydrolyse the peptide bonds of polypeptide chains. They have key roles in digestion, blood clotting, the complement system and in programmed cell death or apoptosis. By forming a covalent acyl-enzyme intermediate, these enzymes hydrolyze peptide bonds by a different pathway to the uncatalyzed reaction, one with multiple steps and a lower free energy of activation.
Describe the role of the active site serine and it activation by the charge relay system.
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some enzymes act as ‘nanomachines’ by converting the energy stored in ATP into mechanical motion, or vice versa.
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