| Hint | Answer | % Correct |
|---|---|---|
| If two enzymes (1: Low Km, 2: High Km) at a metabolic branch point are competing for the same substrate, which one will preferably bind to the substrate? | 1 | 65%
|
| Reusable biological catalysts which speed up chemical reactions | Enzyme | 65%
|
| Name for the chemicals on the right side of a reaction | Product | 61%
|
| What would adding more substrate do to a reaction speed? | Increase | 57%
|
| Name for the chemicals on the left side of a reaction | Substrate | 48%
|
| Enzymatic reaction where 2 molecules are joined with the loss of water | Condensation | 43%
|
| Maximal rate at substrate saturation (expressed as rate of substrate conversion) | Vmax | 43%
|
| Forward and reverse reactions create kinetic ________with equal generation of both substrate/product | Equilibrium | 39%
|
| Which enzyme group adds phosphate groups? | Kinase | 39%
|
| Which type of regulation involves regulator molecules binding (reversibly) to regulatory sites on an enzyme and influencing the binding of substrates to the active site (in a positive or negative manner). | Allosteric | 35%
|
| Reaction involving replacement of one group with another | Substitution | 35%
|
| What is the most common covalent modification, which occurs often at Ser/Thr/Tyr residues? | Phosphorylation | 30%
|
| Substrate concentration for half Vmax (i.e. 50% maximal rate, expressed as concentration) | Km | 26%
|
| Dual oxidation and reduction reactions normally involving Co-Enzymes | Redox | 22%
|
| Enzymatic reaction where 2 molecules are joined together but water is not eliminated, can also happen across a double bond | Addition | 17%
|
| Which enzyme removes phosphate groups? | Phosphatase | 17%
|
| Inhibitors which bind at the active site using a covalent bond and denature the enzyme permanently. | Irreversible | 13%
|
| A reaction pathway which continues in a straight path | Linear | 13%
|
| Inhibitors which do not change the structure of the enzyme and bind to the active or regulatory domains. | Reversible | 13%
|
| Reaction involving transfer of a functional group to a substrate | Transfer | 13%
|
| Enzymatic reaction where a molecule can be split (includes hydrolysis) | Cleavage | 9%
|
| Vmax/Enzyme concentration | Kcat | 9%
|
| Which method do eukaryotic cells use utilizing organelles to create specialised areas within the cell? | Compartmentalization | 4%
|
| A reaction pathway which continues in a cycle, producing by products | Cyclical | 4%
|
| What occurs from a single gene but resulting from PTMs/splice variants etc | Isoforms | 4%
|
| Amount of enzyme which converts 1mole of S to P per min | Kat | 4%
|
| Enzyme activity per mg of protein (measures purity) | Specific activity | 4%
|
| A reaction pathway which splits | Branched | 0%
|
| Chemical modification to the enzyme to increase/decrease activity (e.g phosphorylation, ubiquitinylation) | Covalent control | 0%
|
| What influences the concentration of an enzyme in a cell, which can be altered depending on the availability of substrate. | Genetic expression/Gene level control | 0%
|
| What occurs from different genes generating different proteins? | Isoenzymes | 0%
|
| Amount of enzyme which converts 1umol of S to P per minute | IU | 0%
|
| Reaction involving the changing of position of atoms and functional groups in a molecule | Rearrangement | 0%
|