Enzymes Flashcards

1
Q

How do enzymes effect the rate of reaction

A

Lower activation energy

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2
Q

How do enzymes lower activation energy

A

Entropy reduction
Desolvation
Induced fit

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3
Q

What is entropy reduction

A

Enzymes force substrate into correct orientation by binding in the formation they need to be in for the reaction to proceed

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4
Q

What is desolvation

A

Weak bonds between substrate and enzyme replace most or all H-bonds between substrate and aqueous solution

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5
Q

What is induced fit

A

Substrate binding causes protein conformational change

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6
Q

What is Michaelis-Menten constant

A

Km = substrate concentration when reaction is at ½ the maximum velocity (Vmax)

Km is the concentration of a substrate when the reaction is at half of the max velocity

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7
Q

What does Km and Vmax tell us

A

Km – how specific enzyme is for substrate
Low value = good fit
High value = poor fit i.e. takes a lot of substrate to get to ½ Vmax
Vmax – how fast a reaction is proceeding when enzyme is saturated with substrate

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8
Q

What can affect enzyme reaction

A

Enzyme concentration - how many enzymes available for substrate binding
Substrate concentration - how much substrate is available to bind to enzymes
Temperature - how close/far from optimum
pH - how close/far from optimum
Inhibitors - alter substrate binding

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9
Q

Describe competitive inhibition

A

Inhibitir binds to enzyme active site and prevents binding of substrate
Vmax unchanged
Km increases, takes more substrate to overcome inhibition

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10
Q

Describe non-competitive inhibition

A

Inhibitor binds to secondary site and changes shape of active site
Vmax decreased as many enzymes are not useable
Km remains the same

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11
Q

What is a cofactor

A

non-protein component needed for reaction e.g. magnesium

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12
Q

What is a coenzyme

A

Heat-stable substance that can aid enzyme reactions e.g. FAD from riboflavin

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13
Q

What is a isoenzyme

A

Enzymes that catalyse the same reaction but vary in structure and other biochemical properties

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14
Q

What is a prosthetic group

A

Non-protein group forming part of or combined with a protein.

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15
Q

What is a spontaneous reaction

A

Reaction that favors formation of products at conditions under which reaction is occurring

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16
Q

Why is enzyme activity measured in a clinical setting

A

Detection of suspected disease at pre-clinical stage
Confirmation and assessing severity
Localisation to organs
Characterisation of organ pathology
Assessing response to therapy
Organ function assessment
Assessing genetic susceptibility to drug side effects
Detection of inherited metabolic disease and vitamin deficiencies

17
Q

What factors influence enzyme activity

A

Hypoxia
Cellular damage
Physical damage
Immune disorders
Microbiological agents
Genetic defects
Nutritional disorders

18
Q

What is an allosteric site

A

Site that is different from active site on an enzyme