| Date | May 2017 | Marks available | 1 | Reference code | 17M.1.HL.TZ1.31 |
| Level | Higher level | Paper | Paper 1 | Time zone | Time zone 1 |
| Command term | Question number | 31 | Adapted from | N/A |
Question
The graph shows the rate of an enzymatic reaction versus the substrate concentration, in the absence or presence of an enzyme inhibitor.
Which condition is indicated by lines Y and Z?
Markscheme
C
Examiners report
[N/A]
Syllabus sections
Show 68 related questions
- 17M.2.HL.TZ2.2a: The sketch shows the relationship between the reaction rate and substrate concentration in...
- 17M.1.SL.TZ1.1: Which structure found in eukaryotes has a single membrane? A. Nucleus B. Lysosome C....
- 16N.2.HL.TZ0.3b: Outline the importance of enzymes to metabolic processes.
- 16N.1.HL.TZ0.29: The graph shows an example of an enzyme-catalysed reaction. What does the curve labelled X...
- 16M.1.HL.TZ0.9: In one of the curves in the graph, the rate of an enzyme-catalysed reaction has been plotted...
- 15M.1.HL.TZ1.26: Which describes the role of amino acids in the channels of membrane proteins used for...
- 15M.3.SL.TZ2.9b: Compare competitive and non-competitive enzyme inhibition
- 15M.2.HL.TZ1.2b (i): Identify the protein structures indicated by I and II. I: ...
- 15M.2.HL.TZ1.2b (ii): Describe how structure I is held together.
- 15M.2.HL.TZ1.2b (iii): This protein is described as a globular protein. Distinguish between globular and fibrous...
- 15M.3.SL.TZ1.9b: The enzyme hexokinase catalyses the reaction between glucose and ATP to form Glucose –6–...
- 15N.1.HL.TZ0.10: Once the leaves have been picked, all further metabolism must be stopped. By what means could...
- 15N.2.HL.TZ0.1a: Identify the total number of O. nerka with fork length from 240 to 245 mm caught in autumn...
- 15N.2.HL.TZ0.1b: Compare the data in the graph for autumn 2008 and winter 2009.
- 15N.2.HL.TZ0.1c: Suggest two factors that could affect the distribution of O. nerka in the North Pacific Ocean.
- 15N.2.HL.TZ0.1d: State the range of lipid content measured in O. nerka caught during autumn 2008. .......g
- 15N.2.HL.TZ0.1e: Outline any correlation between total lipid content and fork length in autumn 2008 and in...
- 15N.2.HL.TZ0.1f: Suggest reasons for the differences in lipid content.
- 15N.2.HL.TZ0.1g: Describe the relationship between the distance of upstream migration and the concentration of...
- 15N.2.HL.TZ0.1h: State the concentration of PCBs in muscle lipids at 125 km from the ocean estimated by the...
- 15N.2.HL.TZ0.1i: As the O. nerka migrate upstream they no longer feed. Suggest a reason for the relationship...
- 13M.2.HL.TZ1.3a: State the type of inhibition shown in this diagram.
- 13M.2.HL.TZ2.1f: Determine which sugar is primarily used in the production of ribose.
- 13M.2.HL.TZ1.3b: Explain how this type of regulation could affect the synthesis of an amino acid.
- 13M.2.HL.TZ2.1b: Compare the body fat accumulation between the four groups.
- 13M.2.HL.TZ2.1c: Distinguish between the results for the two groups.
- 13M.2.HL.TZ2.1d: This study also showed a significant reduction in insulin sensitivity when participants were...
- 13M.2.HL.TZ2.1h: Using all of the data, evaluate the evidence that suggests the consumption of large amounts...
- 13M.2.HL.TZ2.1a: Describe the overall trend in body fat accumulation for the four groups of mice.
- 13M.2.HL.TZ2.1e: Discuss whether the results provide clear evidence of a difference in uptake.
- 13M.1.HL.TZ1.27: The enzyme succinic dehydrogenase catalyses the conversion of succinate to fumarate. The...
- 13M.1.HL.TZ2.28: What is an allosteric site? A. The area on an enzyme that binds the end-product of a...
- 13N.1.HL.TZ0.28: What describes non-competitive inhibition?A. Inhibiting molecule does not resemble substrate...
- 13N.2.HL.TZ0.7b: Some proteins in membranes act as enzymes. Describe a model that accounts for the ability of...
- 13M.3.SL.TZ1.8c: Explain non-competitive inhibition.
- 13M.3.SL.TZ2.9a: Distinguish between oxidation and reduction in biological reactions.
- 13N.3.SL.TZ0.7a: State the remaining activity of triose phosphate isomerase when...
- 13N.3.SL.TZ0.7b: Compare the effect of increasing the concentration of peptide 2 and peptide 3 on the...
- 13N.3.SL.TZ0.7c: Identify, with a reason, which of the peptides is the most effective inhibitor of triose...
- 13N.3.SL.TZ0.7d: Deduce, with reasons, whether the peptides act as competitive or non-competitive inhibitors...
- 11M.2.HL.TZ2.5b: Distinguish between competitive and non-competitive enzyme inhibition of chemical reactions,...
- 11M.3.SL.TZ2.8b: Outline the differences between competitive and non-competitive inhibitors.
- 12M.2.HL.TZ1.5c: Explain the effect of inhibitors on the activity of enzymes.
- 12M.2.HL.TZ2.6b: Outline control of metabolic pathways.
- 12M.1.HL.TZ1.26: A substrate undergoes a series of enzyme-catalysed reactions to form intermediate substances...
- 12M.1.HL.TZ1.27: What effect would adding an enzyme have on energy changes during the reaction? A. Reduce...
- 12M.1.HL.TZ2.27: How does a competitive inhibitor interact with an enzyme? A. It binds to the active site,...
- 12M.3.SL.TZ2.8c: Describe non-competitive inhibition.
- 12M.3.SL.TZ2.7a: State the relationship between Rubisco activity and temperature.
- 12M.3.SL.TZ2.7c: Determine which enzyme shows overall greater activity from 25°C to 42°C.
- 12M.3.SL.TZ2.7d: Explain the change in activase activity at temperatures higher than 42 °C.
- 12M.3.SL.TZ2.7e: In a leaf, both enzymes are present together. Predict, with a reason, how the rate of...
- 09M.2.HL.TZ1.6c: Outline how enzymes catalyse reactions.
- 10M.1.HL.TZ1.27: Which is correct for the non-competitive inhibition of enzymes?
- 10M.1.HL.TZ2.27: Why is oxaloacetate a competitive inhibitor? A. It causes a conformational change to the...
- 10M.3.SL.TZ1.12: Explain the control of metabolic pathways.
- 09N.1.HL.TZ0.26: The graph below shows energy changes during a chemical reaction that occurs without a...
- 11N.3.SL.TZ0.9c: Explain the control of metabolic pathways by end-product inhibition.
- 11N.3.SL.TZ0.8c: Distinguish between oxidation and reduction.
- 12N.1.HL.TZ0.26: The diagram represents an allosteric enzyme. Where would the following inhibitors be most...
- 12N.1.HL.TZ0.25: The following graph shows energy changes with and without enzymes during a chemical...
- 12N.3.SL.TZ0.8a: Describe how the tertiary protein structure relates to enzyme function.
- 12N.3.SL.TZ0.8b: Explain the control of metabolic pathways by end-product inhibition, including the role of...
- 10N.3.SL.TZ0.7c: Explain why the activity of the enzyme from wild-type plants changes when the inhibitor is...
- 10N.3.SL.TZ0.7a: State the activity of the wild-type enzyme without the inhibitor and with the...
- 10N.3.SL.TZ0.7b: Distinguish between the enzyme activity without the inhibitor in the wild-type and the mutant...
- 10N.3.SL.TZ0.7d: The scientists concluded that the enzymes of the mutant plants had a reduced activity, but...
- 09N.3.SL.TZ0.8c: Explain what is meant by allosteric inhibition.
