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OCR Biology A - 2.1.4 - Enzymes Part 1

Biology20 CardsCreated about 1 month ago

This deck covers key concepts about enzymes, including their properties, mechanisms, and roles in biological processes. It includes definitions, hypotheses, and examples of enzyme regulation and inhibition.

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What does a substrate need to have in order to bind with an active site?

Complementary shape Opposite charges to the active site
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Key Terms

Term
Definition
What does a substrate need to have in order to bind with an active site?
Complementary shape Opposite charges to the active site
How does change in pH alter the rate of the reaction?
Electric charges of both the enzyme and substrate are neutralised by the presence of either positive or negative ions so no enzyme-substrate complex i...
Allosteric enzyme regulation?
An inhibitor can bind to the allosteric site and usually inhibits the activity However Cyclic AMP can bind to the inhibitor and remove it so the enzym...
Competitive inhibition?
Competitive inhibitors compete with the substrate to bind with the active site Has sim shape to part of/all of substrate A competitive inhibitor occup...
Non-competitive inhibition?
Non competitive inhibitors binds with the enzyme at allosteric site. Inactivates the enzyme by altering shape (changes 3’ structure) Can be irreversib...
Why are heavy metals (e.g. lead and arsenic) poisonous?
They have such strong affinities for - SH (sulfhydryl) groups and destroy catalytic activity
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OCR Biology A - 2.1.4 - Enzymes Part 1
TermDefinition
What does a substrate need to have in order to bind with an active site?
Complementary shape Opposite charges to the active site
How does change in pH alter the rate of the reaction?
Electric charges of both the enzyme and substrate are neutralised by the presence of either positive or negative ions so no enzyme-substrate complex is formed
Allosteric enzyme regulation?
An inhibitor can bind to the allosteric site and usually inhibits the activity However Cyclic AMP can bind to the inhibitor and remove it so the enzyme can be active again
Competitive inhibition?
Competitive inhibitors compete with the substrate to bind with the active site Has sim shape to part of/all of substrate A competitive inhibitor occupies the active site only temporarily and so the reaction is reversible Doe not change Vmax
Non-competitive inhibition?
Non competitive inhibitors binds with the enzyme at allosteric site. Inactivates the enzyme by altering shape (changes 3’ structure) Can be irreversible
Why are heavy metals (e.g. lead and arsenic) poisonous?
They have such strong affinities for - SH (sulfhydryl) groups and destroy catalytic activity
How is enzyme inhibition exploited to control disease?
Penicillin and other drugs inhibit enzymes that certain diseases use in order to survive
2 types of enzymes?
Intracellular (catalase, converts H2O2 into O2 and H2O) Extracellular (digestive enzymes)
Properties of enzymes?
Complementary active site to shape of substrate High turnover no. Ability to reduce activation energy Left unchanged after reaction
What are enzymes affected by?
Temperature pH Enzyme conc. Substrate conc.
Lock and key hypothesis?
Shape of active site caused by sequence of amino acids (specific tertiary structure - 3D)
Induced fit hypothesis?
Explains how activation energy is reduced Active site is not perfectly complementary but when substrate moves into active site, interferes with the bonds holding active site together Induces changes in 3’ structure to strengthen binding and weaken bonds in substrate Active site alters to give perfect fit. Changed shape of active site —> bonds in substrate easier to make or break (reduces activation energy)
Enzyme controlled reaction?
Enzyme + substrate (E + S) —> enzyme substrate complex (ESC) —> enzyme product complex (EPC) —> Enzyme and product (E + P)
Effects of pH on enzymes?
Enzymes fully denatures before pH 3 and after pH 11 Enzymes start to denature after pH 7 Hydrogen ions that cause acidity affect interaction between polar and charged R groups and alter tertiary structure
Co-enzymes?
Small, organic, non protein molecules that bind to active site for short time Take part in reaction and is recycled Can carry chemical groups
Example of co-enzymes?
FAD NAD Co-enzyme A Vitamin B3 - helps break down carbs and fat
Prosthetic groups?
Co-enzyme that is a permanent part of an enzyme molecule (inorganic ion) Found in conjugated protein molecules e.g. haemoglobin (Fe^2+) Contribute to final 3D shape and charge
Example of prosthetic groups?
Carbonic anhydrase contains a zinc based prosthetic group, helps catalyse CO2 and H2O to make carbonic acids (found in rbc)
Co-factors?
Presence of certain ions increase reaction rate Ions combined with an enzyme or substrate Binding helps form an ESC more easily, affects shape and charge e.g. Cl- helps form active site to amylase
How are hydrogen bonds formed?
The slight -ve charge on the oxygen atom attracts the slight +ve charge on a hydrogen atom forming a strong bond