Term
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Definition
| biological catalysts composed of RNA instead of peptides |
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Term
| What are the six major groups of enzymes? |
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Definition
- lyases
- isomerases
- ligases
- hydrolases
- oxidoreductases
- transferases |
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Term
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Definition
| catalyze redox reactions; common cofactors are NAD+ and heme |
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Term
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Definition
| move a functional group from one molecule to another; named as trans[functional group]ase or [functional group] transferase |
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Term
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Definition
| catalyze cleavage without the addition of water; phosphatase, peptidases, nucleases, lipases |
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Term
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Definition
| catalyze cleavage without the addition of water and without the transfer of electrons. The reverse reaction (synthesis) is often more important biologically; synthases |
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Term
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Definition
| catalyze the interconversion of isomers, including both constitutional isomers and stereoisomers; some can also be classified as other enzyme types depending on mechanism |
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Term
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Definition
| responsible for joining two large biomolecules, often of the same type |
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Term
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Definition
| hypothesizes that the enzyme and substrate are exactly complementary |
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Term
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Definition
| hypothesizes that the enzyme and substrate under undergo conformational changes to interact fully |
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Term
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Definition
- small organic groups, mostly vitamins or vitamin derivatives (NAD, FAD, coenzyme A)
- generally inorganic molecules or metal ions
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Term
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Definition
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Term
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Definition
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Term
| Michaelis-Menten equation |
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Definition
v = (vmax[S])/(Km + [S])
Km = 1/2vmax
Km is the Michaelis Constant
[S] is substrate concentration
vmax is the maximal reaction velocity
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Term
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Definition
| Km is a measure of substrate enzyme affinity, a higher Km equals a lower affinity |
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Term
| Reading Lineweaver-Burke Plots |
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Definition
- x-intercept equals -1/Km
- y-intercept is the vmax
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Term
| What is the optimal pH of the blood, stomach and small intestine? Why does it matter? |
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Definition
| 7.4, 2 and 8.5; it is important for the function of the enzymes in that part of the body |
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Term
| What are the four types of reversible inhibition? |
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Definition
- competitive
- noncompetitive
- mixed
- uncompetitive
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Term
[image]
What kind of inhibition is this? |
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Definition
| competitive inhibition, vmax stays the same, Km increases (meaning enzyme-substrate affinity decreases); this type can be overcome by adding more substrate; inhibitor binds the active site |
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Term
[image]
What kind of inhibition is this? |
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Definition
| noncompetitive inhibition - decreases Vmax, Km stays same, binds to allosteric site inducing change in enzyme conformation |
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Term
[image]
what kind of inhibition is this? |
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Definition
| uncompetitive inhibition - bind only to enzyme-substrate complex locking them together and preventing their release; lowers Km and vmax |
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Term
[image]
What kind of inhibition is this? |
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Definition
| mixed inhibition - binds allosteric site and preferentially binds enzyme (increases Km) or enzyme substrate complex (decreases Km); vmax decreases in both cases |
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