Enzymes SAC Mindmap

Minoshka Bocarro
Mind Map by Minoshka Bocarro, updated more than 1 year ago
Minoshka Bocarro
Created by Minoshka Bocarro about 4 years ago
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Mind map of the concepts under enzymes
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Enzymes SAC Mindmap
1 Experimental Methods of Study of Enzyme Action
1.1 Rate
1.1.1 Quantity over time (divided by)
1.2 Displacement
1.2.1 Something gets replaced
1.3 Does the reaction naturally occur?
1.3.1 Yes but at a such a slow rate that nothing occurs
1.4 Independent
1.4.1 Usually stems for the factors that affect enzyme rate even if not explicitly stated
1.4.1.1 pH
1.4.1.2 Temperature
1.4.1.3 Enzyme or substrate concnetration
1.4.1.4 Inhibition
1.4.1.5 Volume of container
2 Analysing, Interpreting and Evaluating the Results and Procedures of the Practical Investigation
2.1 experimental design
2.1.1 hypotheisis
2.1.1.1 cause and effect
2.1.1.1.1 Independent and dependent variables
2.1.2 variables
2.1.2.1 Indpendent
2.1.2.1.1 Include a range
2.1.2.1.1.1 See overall trend of the relationship
2.1.2.1.1.2 Show variation
2.1.2.2 Dependent
2.1.2.3 Controlled
2.1.2.3.1 Constant
2.1.2.3.1.1 Fair test as only one variable is affecting the outcome
2.1.2.3.2 Specifically state what is controlled
2.1.2.3.2.1 Temperature of enzyme or of substrate?
2.1.3 Method
2.1.3.1 Use an annotated diagram to quickly demonstrate the process
2.1.3.2 Repetitions
2.1.3.2.1 Minimal 10
2.1.3.2.2 Fair test - Rule out any errors and affirm that a trend occurs
2.1.4 Results
2.1.4.1 Qualitative
2.1.4.1.1 Support quantitative data
2.1.4.1.1.1 Verify that any mistakes were due to error and method was done properly
2.1.4.2 Quantitative
2.1.4.2.1 More accurate
2.1.4.2.2 Precision
2.1.5 Control Group
2.1.5.1 Comparison point for ---
2.1.5.1.1 Confirms that independent conducted the change
2.1.5.2 Multiple Control groups
2.1.5.2.1 If points needed for comparison
3 Terms, concepts and Relationships
3.1 Enzyme Catalysed Reactions
3.1.1 Roles
3.1.1.1 Increase the rate of the reactions
3.1.1.1.1 Decrease the activation energy required to reach the transition state
3.1.1.1.1.1 A.K.A the state in which the reaction begins
3.1.1.1.1.1.1 weakening of bonds
3.1.1.1.1.1.1.1 How does it do this?
3.1.1.1.1.1.1.1.1 Brings bonds closer together?
3.1.1.2 Able to be reused over and over again until worn out
3.1.1.2.1 Thus able to be used in small amounts
3.1.1.3 Can occur in both directions of the reaction. Catabolic and anabolic
3.1.1.3.1 Needs different enzymes to do so though
3.1.2 Mode of Action
3.1.2.1 Induced Fit
3.1.2.1.1 Enzyme Substrate Complex
3.1.2.1.1.1 not exact fit. Shows enzymes flexibility, conform=complementry shape
3.1.2.1.1.1.1 when disassociated=returns to original shape
3.1.2.2 Lock & KEy
3.1.2.2.1 Enzymes Substrate Complex
3.1.2.2.1.1 requires an exact fit
3.1.3 Inhibition
3.1.3.1 Rational Drug Design
3.1.3.2 TYPE
3.1.3.2.1 COMPETITIVE
3.1.3.2.1.1 Directly binds with the active site.
3.1.3.2.1.1.1 Blocks the substrate from interacting with the enzyme
3.1.3.2.1.2 If reversible
3.1.3.2.1.2.1 higher concentrations of substrate can dislodge it
3.1.3.2.1.3 If not reversible
3.1.3.2.1.3.1 accumulation can occur
3.1.3.2.2 NON-COMPETITIVE
3.1.3.2.2.1 Does not bind to the active site but to another part of the enzyme. However slightly changes the shape of the enzyme and active site
3.1.3.2.2.2 Can not be removed
3.1.3.2.2.2.1 permanent or cant be removed by substrate
3.1.4 Location
3.1.4.1 Intracellular
3.1.4.2 Extracellular
3.1.5 Factors affecting enzyme rate
3.1.5.1 Natural
3.1.5.1.1 COFACTORS and COENZYMES
3.1.5.1.1.1 can help produce a better fit of the enzyme-substrate complex
3.1.5.1.1.2 Coenzymes = Vitamins
3.1.5.2 Increased Concentration of Substrates
3.1.5.2.1 Saturated
3.1.5.2.1.1 All active sites are occupied
3.1.5.3 Temperature
3.1.5.3.1 Affect collision rate of enzymes with substrates
3.1.5.3.1.1 Optimal Temperature
3.1.5.3.1.1.1 Highest enzyme activity
3.1.5.3.1.1.1.1 Too much below
3.1.5.3.1.1.1.1.1 Inactive
3.1.5.3.1.1.1.1.1.1 Snow movement, not as much or no collisions
3.1.5.3.1.1.1.2 Too much above
3.1.5.3.1.1.1.2.1 Denatured
3.1.5.3.1.1.1.2.1.1 Heat affects tertiary structure of enzyme and unfolds
3.1.5.4 pH
3.1.5.4.1 Affect attraction of active site and therefore binding
3.1.5.4.1.1 Hydrogen ions
3.1.5.4.1.1.1 Extreme High
3.1.5.4.1.1.1.1 Denature
3.1.5.4.1.1.2 Extreme Low
3.1.5.4.1.1.2.1
3.1.5.4.1.1.3 Optimal pH
3.1.5.4.1.1.3.1 Highest enzyme activity
3.1.5.4.1.1.3.2 Varies per enzyme
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