Term
What Maintains a narrow range of cellular temps
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Definition
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Term
| organisms that live in an environment with higher than average temperatures for biotic life |
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Definition
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| What type of bacteria can live in an environment with the temperature averaging 70 degrees Celsius |
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| What has enzymes that operate at high temperatures and are critical to bio-technology? |
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Definition
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| Give an example of how thermophiles contribute to bio technology? |
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Definition
| PCR and/or DNA sequencing |
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| What is the name of the thermophilic bacteria that is the driving force of PCR and DNA Sequencing? |
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Definition
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Term
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Definition
| Polymerase Chain Reaction |
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Definition
| This chart shows enzyme activity in relation to temperature. It compares the optimal temperature for human enzymes vs optimal temperature for thermophile enzymes. |
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Term
| What is the pH range that most enzymes can be active between? |
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Definition
| They can be active within 3 to 4 pH units |
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Term
| Name two human digestive enzymes? |
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Definition
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Term
| What is the active pH for Pepsin? And where can it be found? |
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Definition
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Term
| What is the active pH of trypsin? And where is it found? |
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Definition
| In the intestines, pH of 8 |
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Term
| Name some commonly important ions? |
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Definition
| Na, Zn, K, PO4, H+, Cl, Mg, Mn, NH3 |
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| Magnesium and Calcium are in low concentration compared to the other ions, what should this make you think? |
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Definition
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Term
| What is the number of substrate molecules converted to product per unit time called? |
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Definition
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Term
| When increasing the amount of enzyme available in a reaction what will this also increase? And why? |
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Definition
| Increases the turnover rate because more substrate can be catalyzed per unit time |
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Definition
This graph shows the relationship between enzyme concentration and reaction rate.
The line shows a linear increase, meaning that there is an unchanging substrate concentration. |
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Definition
This graph shows the relationship between Substrate concentration and Reaction Rate.
X being the point of saturation.
The increasing concentration does not affect reaction rate. There is a constant enzyme concentration. The enzyme present is saturated aka always bound to substrate |
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Term
| Enzymes are critically affected by what? (name 3 things) |
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Definition
| concentrations of substrates, products, and inhibitors present in the cell |
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Term
| What could you add to a reaction to increase the rate? |
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Definition
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Term
| What is it called when the inability of increasing substrate concentrations to increase the velocity beyond a finite upper value? |
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Definition
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Term
| When do enzymatic reactions become saturated? |
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Definition
| at high substrate concentrations |
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Definition
This is the Michaelis-Mentan (M&M) equation.
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Term
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Definition
| This graph shows the hyperbolic relationship between [S] and v |
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Term
| In the M&M equation what does Vmax mean? |
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Definition
| Vmax is the max rate in which a product is formed |
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Term
| In the M&M equation what does [S] mean? |
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Definition
| initial concentration of substrate |
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Term
| In the M&M equation what does Km mean? |
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Definition
| the concentration of substrate at which initial velocity = 1/2 Vmax |
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Term
| In the M&M equation what does v mean? |
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Definition
| initial reaction velocity at that substrate concentration |
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Term
| When you have a very high substrate concentration and a low Km.... [S]>> Km, what will V equal? |
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Definition
V= Vmax
It is saturated.
Turnover rate |
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Term
When substrate concentrations equal Km..[S]= Km
what will V equal? |
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Definition
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Term
| When you have a very low substrate concentration [S]<<Km....what will V equal |
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Definition
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Definition
High Km means low affinity
Low Km means high affinity |
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Term
| Given: Enzyme A: Km=15mM Enzyme B: Km=5mM Which one will happen first and which one has a higher affinity? |
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Definition
| Enzyme A will happen 1st. Enzyme B has a higher affinity |
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Term
| What is termed the Michaelis constant? |
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Definition
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Term
| What kind of plot would you need to accurately determine the value of Km and Vmax, since them M&M hyperbolic representation makes it too hard to determine? |
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Definition
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Term
| Who converted the hyperbolic relationship into a linear function? |
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Definition
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Definition
This is an example of a double reciprocal plot.
This allows for accurate determination of Vmax and Km values |
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Term
| Name some things that may have an affect on enzyme inhibition? |
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Definition
| Drugs, toxins, alternative substrates, substrate analogs, and allosteric effectors |
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Term
| Inhibition is not necessarily harmful but is considered a common method of what? |
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Definition
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Term
| What term describes reducing the reaction rate with the desired substrate? |
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Definition
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Term
| What do Irreversible inhibitors do to the enzyme? |
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Definition
| They are usually toxic to the cells, they bond covalently causing irrevocable loss of catalytic activity |
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Term
| What are some examples of irreversible inhibition? |
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Definition
diisopropyl fluorophosphate (a nerve gas)
Physotigmine (an alkyloid from a calabar bean, toxic)
Penicillin (affects cell wall synthesis) |
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Term
| What enzyme is vital for the transmission of nerve impulses? |
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Definition
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Term
| What would happen if Acetylcholinesterase was inhibited? |
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Definition
| could lead to rapid paralysis of vital function and therefore to death |
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Term
| How does the inhibition of acetylcholinesterase happen? |
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Definition
| When acetylcholine is on a neuron receptor, acetylcholinesterase comes in and breaks it down, releasing it from the receptor. But when inhibited it cannot be taken off the receptor. |
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Term
| Which example if irreversible inhibition leads to permanent enzyme inactivity? |
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Definition
| The nerve gas does. You have to make new enzymes before you can fix the issue |
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Term
| What kind of inhibitor can be in equilibrium? |
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Definition
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Term
There are 3 categories that are separated by location of binding to the enzyme, list them.
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Definition
| 1. Competitive Inhibitors 2. Noncompetitive Inhibitors 3. Uncompetitive Inhibitors |
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Term
| Which kind of inhibitor competes with substrate binding at the active site but cannot be catalyzed? |
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Definition
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Term
| What kind of inhibitor reduces enzyme activity by preventing substrate binding? |
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Definition
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Term
| Are Competitive Inhibitors reversible or irreversible? |
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Definition
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Term
| With Competitive Inhibitors, how can you overcome the affects of the inhibitors? |
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Definition
| By increasing the substrate in the environment |
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Term
| Which two Inhibitors deals monomeric enzymes? |
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Definition
| Competitive and Noncompetitive |
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Term
| Which kind of inhibitor cannot bind at enzymes active site, but bind on another location on the enzyme? |
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Definition
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Term
| Are Noncompetitive Inhibitors reversible or irreversible? |
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Definition
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Term
| With Noncompetitive Inhibitors, can you overcome the affects of the inhibitors by increasing substrate concentration? |
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Definition
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Term
| What binds to ES complex and prevents catalysis |
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Definition
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Term
| What term is applied to chemicals designed to closely resemble substrate so they can bind at an enzymes active site while being uncatalyzable? |
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Definition
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Term
| Name two common enzyme regulation methods? |
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Definition
| Substrate Regulation and Allosteric Regulation |
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Term
| Those mechanisms that depend directly on substrate-enzyme interactions are termed? |
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Definition
| Substrate-level regulation |
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Term
| Name four examples of substrate level regulation |
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Definition
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Term
| What type of regulation deals with at least a dimer? |
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Definition
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Term
| When enzymes exist in two different shapes means they are regulated by? |
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Definition
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Term
| Describe what affects the two shapes, in allosterics, have. |
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Definition
| One form the enzyme has high affinity for substrate = high reaction rates And in the other form the enzyme has little or no affinity for substrate= no reaction rate |
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Term
| What determines the shape of the enzymes is determined by what two things? |
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Definition
| the presence and binding of appropriate regulatory substances called allosteric effectors |
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Term
| What causes a reversible alteration in the enzymes conformation? |
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Definition
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Term
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Definition
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Term
| The allosteric site is located on what domain? |
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Definition
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Term
| Allosteric effectors that increase enzyme function when they bind are called? |
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Definition
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Term
| Effectors that inhibit enzymes when the bind are called/ |
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Definition
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Term
| Give an example of a allosteric inhibitor and an allosteric activator |
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Definition
Inhibitor....ATP
Activator...ADP |
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Term
| What is the overall idea of what an effector does? |
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Definition
| changes how an enzyme works |
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