Term
From the equations, what is ?
Km |
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Definition
| Km = Michaelis constant - shows dissociation |
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Term
From the equations, what is ?
[S] |
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Definition
| [S] = Substrate concentration |
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Term
From the equations, what is ?
[P] |
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Definition
| [P] = Product concentration |
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Term
From the equations, what is ?
[ES] |
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Definition
| [ES] = Enzyme-substrate concentration |
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Term
From the equations, what is ?
Vmax
What 2 things mutliplied give = Vmax? |
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Definition
Vmax = Rate of reaction when enzymes are fully saturated with substrate
Vmax = (E)(k2) |
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Term
From the equations, what is ?
V0 |
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Definition
V0 = The rate of formation of product
(big equation in Michaelis-Mentis model) |
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Term
| What is the Michaelis-Mentis Equation? |
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Definition
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Term
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Definition
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Term
| What defines the slope in the double reciprocal or lineweaver-burk plot ? |
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Definition
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Term
From the equations, what is ?
Kcat |
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Definition
| Kcat (or K2, same thing) is the 'turnover number' the number of molecules of substrate converted into product in an active site when fully saturated |
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Term
| Explain Sequential Reactions |
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Definition
| Sequential reactions begin with subtrates A&B and an Enzyme. A&B attach to the enzyme to form a ternary complex, and then are released as modified products C&D. E is unchanged. |
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Term
| Explain Double Displacement (pingpong) reactions |
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Definition
| Double displacement reactions involve substrate A adding to the enzyme, and being released as product B, BUT the enzyme is slightly modified. The slightly modified enzyme can then bind to another substrate (C), and release it as product D before becoming the original enzyme again. |
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Term
What are the terms that characterize/define:
Double displacement reactions
Sequential reaction |
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Definition
Double displacement reaction - The Substituted Enzyme Intermediate
Sequential - The Ternary complex |
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Term
| What effect does a noncompetitive inhibitor have on the Vmax, and Km |
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Definition
| Noncompetitive inhibitors don't change the Km, and decrease the Vmax |
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Term
| What effect does a competitive inhibitor have on the Vmax, and Km |
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Definition
| A competitve inhibitor increases the Km, and doesn't affect the Vmax |
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Term
Irriversible inhibitors:
How do group-specific reagents work? |
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Definition
| Group specific reagents react with specific amino acids |
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Term
Irriversible inhibitors:
How do affinity labels (reactive substrate analogs) work? |
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Definition
| They are molecules that are similar to the substrate for the enzyme and that covalently bind to the active-site residues. They modify the enzyme such that it is irriversibly inhibited. |
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Term
Irriversible inhibitors:
How do suicide inhibitors (or mechanism-based inhibitors) work? |
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Definition
| The molecule binds to the substrate and generates a CHEMICALLY reactive intermediate (becomes oxidized/reduced) that inactivates the enzyme through covalent modification. |
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Term
Irriversible inhibitors:
How do suicide inhibitors (or mechanism-based inhibitors) work? |
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Definition
| The molecule binds to the substrate and generates a CHEMICALLY reactive intermediate (becomes oxidized/reduced) that inactivates the enzyme through covalent modification. |
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Term
Irriversible inhibitors:
How do transition state analogs work ? |
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Definition
| Compounds resembling the transition state of a catalyzed reaction effectively inhibits enzymes |
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Term
Allosteric Enzymes -
Do they obey Michaelis-Menten model ?
Do they involve a greater # of units ?
What kind of plot do they display ?
What kind of binding pattern do they undergo ?
Are they reversible or irriversible? |
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Definition
Allosteric Enzymes-
They DO NOT obey the Michaelis-Menten model
They involve a greater # of subunits (quaternary), and thus more active sites
They display sigmoidal plots
They follow a co-operative binding pattern
Typically reversible |
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Term
Allosteric Enzymes-
Explain the sequential model. |
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Definition
| The enzyme starts in TT form. The sequential model fills one active site with substrate switching it to RT form, and then the second one attaches as well switcing it to RR form. |
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Term
Allosteric Enzymes-
Explain the concerted model. |
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Definition
| The enzyme starts in TT form. The concerted model fills one active site with substrate switching the enzyme to R form (high affinity) |
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Term
Allosteric Enzymes -
What do Inhibitors and activators do? |
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Definition
Allosteric Enzymes-
Inhibitors change the enzyme from R state to T State
Activators change the enzyme from T state to R state
T state is low affinity
R state is high affinity |
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Term
| How does Penicillin work ? |
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Definition
| Penicillin destroys the cell wall of the microorganism by deactivating the enzyme that is required to crosslink the cell walls. |
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Term
What kind of inhibitor is Penicillin ?
What is the enzyme that it attaches to? |
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Definition
Penicillin is a suicide inhibitor.
The enzyme it attaches to is transpeptidase. |
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Term
| Name 4 water soluble Vitamins |
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Definition
Vitamin B5 - Pantothenate
Vitamin C - Ascorbic Acid
Vitamin B3 - Viacin
Vitamin B6 - Pyridoxine |
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Term
| Name 4 lipid soluble Vitamins |
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Definition
Vitamin K1
Vitamin A - Retinol
Vitamin E - alpha Tocopherol
Vitamin D2 - Calciferol |
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Term
Name the consequence of deficiency of the following:
Vitamin K1
Vitamin A - Retinol
Vitamin E - alpha Tocopherol
Vitamin D2 - Calciferol |
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Definition
Deficiency of, causes:
Vitamin K1
*blood clotting problems
Vitamin A - Retinol
*lacking vision
Vitamin E - alpha Tocopherol
*becomes deactive in lipid membranes
Vitamin D2 - Calciferol
*no calcium Regulation |
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