energetics and enzymes Flashcards

enzyme catalysis: explain how enzymes act as catalysts of reactions. Draw graphs to show the effects of substrate concentration, temperature and pH on reactions catalysed by enzymes

1
Q

define enzyme

A

protein acting as catalyst to induce chemical changes in other substances, but remains unchanged by process; increases rate or reaction; high specificity; delta G remains same but lowers Ea

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2
Q

hydrolase

A

catalyse hydrolytic cleavage

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3
Q

dehydrogenase

A

oxidise substrate by reducing coenzyme

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4
Q

protease

A

hydrolyse peptide bonds

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5
Q

nuclease

A

hydrolyse phosphodiester bonds

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6
Q

ligase

A

joins two molecules together

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7
Q

transferase

A

transfer functional groups

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8
Q

isomerase

A

rearrange bonds within molecule

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9
Q

polymerase

A

catalyse polymerisation reactions

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10
Q

kinase

A

catalyses phosphorylation and activation

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11
Q

phosphatase

A

hydrolytic removal of phosphate

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12
Q

oxido-reductase

A

one oxidised, one reduced (type of dehydrogenase)

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13
Q

ATPase

A

hydrolyses ATP

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14
Q

glucose-6-phosphatase

A

catalysed aq reaction of glucose-6-phosphate with water to form glucose and Pi

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15
Q

lysozyme: function

A

hydrolyses B(1-4) bond in peptidoglycan (NAG and NAM) so bacteria lyse and die

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16
Q

requirements of Glu-35 and Asp-52 to ensure maximum rate of lysozyme hydrolysis

A

Glu-35 is protonated and Asp-52 is ionised, so +ve transition can be stabilised

17
Q

mechanism of Glu-35 and Asp-52

A

Glu-35 protonates the oxygen in the glycosidic link between the two sugars, breaking the glycosidic bond; water molecule enters and is deprotonated by Glu-35; Asp-52 stabilises the positive charge in the transition state; OH- attacks the remaining sugar molecule, adding an OH group to it; proton is transferred to Glu-35 to return it to it’s original state; Glu-35 and Asp-52 are both in their original state to continue catalysis

18
Q

lock and key hypothesis

A

substrate shapes exactly complementary to active site

19
Q

induced fit hypothesis

A

substrate induces change in active site (proteins possess degree of flexibility)

20
Q

effect of pH on catalysed reactions

A

optimum pH, sharp decrease either side as enzyme denatures

21
Q

effect of T on catalysed reactions

A

slow increase in rate as gain kinetic energy, optimum T, rapid decline as enzyme active site denatures

22
Q

effect of [substrate] on catalysed reactions

A

increases until [enzyme] or other factors become limiting