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Definition
Most reactions, both forward and backward, are increased by this factor |
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Definition
Number of biochemical reactions known to have a specific enzyme for enhancement |
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Definition
Number of total enzymes known |
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Definition
These modulate enzyme activity |
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Activators and Inhibitors |
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Definition
These are 2 types of effectors |
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Term
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Definition
Most enzymes have a _______ for a narrow range of substrates |
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Term
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Definition
Enzymes bind to substrates at the |
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Term
Type and Arrangement of amino acid R-group in active site |
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Definition
This determines the substrate molecule that can bind and react |
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Term
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Definition
How many R-groups per active site? |
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Term
Non-covalent cofactors and covalent prosthetic groups |
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Definition
These are not protein molecules associated with the enzyme on or near the active site; They help to determine substrate specificity |
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Which of 6 major enzyme classes |
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Definition
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Definition
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Subclass of bond type and group transfer |
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Definition
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Definition
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Term
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Definition
This enzyme catalyzes the phosphorylation of D-glucose |
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Term
E.C. 1; Catalyzes redox reactions, proton or electron donor is one of the substrates |
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Definition
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Term
E.C. 2: Catalyzes group treasfer |
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Definition
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Term
E.C. 3: Catalyzes the hydrolytic cleavage of C-C, C-N, C-O, etc. |
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Definition
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E.C. 4: Catalyzes non-hydrolytic cleavage of C-C, C-N, C-O; adds a double bond or addition to a double bond |
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Definition
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E.C. 5: Catalyzes molecular geometry re-arrangement; transfer of groups to yield isomeric forms |
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Definition
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Term
E.C. 6: Ligation (joining) of 2 molecules with hydrolysis of increased energy bond (condensation coupled to ATP hydrolysis) |
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Definition
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Term
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Definition
Energy for reaction to proceed is called |
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Definition
Binding of enzyme to substrate ___ activation energy |
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Term
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Definition
Rate of Reaction depends upon how efficiently the reactants meet the ____ _____. |
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Term
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Definition
This is an unstable, energized atom where bonds are broken and formed |
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Term
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Definition
Reactants are normally in this state and have little potential energy |
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Term
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Definition
This is how long the transition state is stable. |
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Term
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Definition
This is the stable structure that resembles postulated transition state |
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Term
Facilitation of Proximity (Propinquity Effect) |
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Definition
The reaction rate of reaction is increased when enzyme removes molecules from dilute solution and holds them close together in enzyme active site |
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Term
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Definition
Rate of reaction is increased when amino acid in active site with aliphatic R-group of enzyme attacks electrophilic substrate, forming a covalent bond between enzyme and substrate |
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Term
COO, NH2, aromatic OH, histidyl groups, R-OH, S |
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Definition
6 groups that can act as nucleophiles |
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Term
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Definition
Increses the rate of reaction by a transfer of a proton in the transition state |
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Term
GLU, HIS, LYS, ASP, TYR, CYS |
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Definition
Amino Acids that act as acid catalysts when pronated |
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Term
pKa of active site and enzymes optimum pH |
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Definition
Acid Base Catalysis depends on these two factors |
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Term
Molecular Distortion and Strain |
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Definition
Increase in the rate of reaction when the strain induced in bond systems of reactants is released when the transition state converts to products |
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Term
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Definition
States that an increased concentration of reactants equals an increased reaction rate |
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Term
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Definition
This is another term for the initial period. |
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Definition
Reaction achieves this when the E.S. and concentration of any other intermediates remain constant |
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Definition
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Term
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Definition
Catalytic rate, or product formation rate |
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Definition
Measures the number of molecules turned per enzyme per molecule per second |
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Term
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Definition
This is the Michaelis Menten equation |
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Term
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Definition
Michaelis Menten constant |
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Term
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Definition
Equation for the rate of product formation |
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Term
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Definition
Equation for the rate of product breakdown |
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Term
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Definition
The initial velocity of a reaction reflects a steady state where ES is constant or ES formation is equal to ES breakdown |
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Term
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Definition
This equation is only true when Vmax is equal to 1/2Vo |
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Term
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Definition
A direct measure of reaction efficiency can be measured by |
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Term
Theoretical Max Efficiency |
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Definition
This is the term for when every collision of E and S gives ES |
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Term
1/Vo= (km/Vmax)(1/[S]) + (1/Vmax) |
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Definition
Limeweaver Burke Equation |
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Term
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Definition
If a reaction is using more than one substrate, this is different for each substrate. |
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Term
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Definition
This type of reaction involves the transfer of one atom or a group from one substrate to another substrate. |
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Term
Random Binding and Ordered Binding |
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Definition
What are the 2 types of ternary complex formation? |
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Term
Ternary Complex Formation (Ordered and Random Binding) and Ping Pong/Double Displacement |
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Definition
What are the two types of bisubstrate reactions? |
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Term
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Definition
This occurs when an inhibitor molecule looks like substrate and competes for binding at active site |
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Term
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Definition
If this is increased in competitive inhibition, probability of I binding is minimized and the reaction has a normal Vmax |
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Term
When the enzyme denatures. |
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Definition
Enzymatic reactions behave similarly up to this point. |
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Term
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Definition
Which is more stable? Low MW enzymes, or high MW enzymes? |
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Term
They shake apart because they are held together by weak interactions. |
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Definition
Why are high MW less stable? |
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Term
The relationship between k and Ea |
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Definition
What does the Arrhenius Equation show? |
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Term
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Definition
This effects the ionizable state; it influences active site structures and effects enzyme efficiency |
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Term
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Definition
RNA that behave like enzymes. |
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Term
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Definition
Surface Dilution Kinetics enzymes have these kinds of substrates, activators, and inhibitors. |
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Term
Surface Dilution Kinetics |
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Definition
This model takes into account surface concentration of lipids and bulk concentration |
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Term
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Definition
This system is used in assaying lipid dependent enzyme activity. |
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Term
Non-ionic detergent Triton X-100 and lipids |
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Definition
Mixed Micelle is composed of these two components. |
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Term
Bulk concentration and Surface Concentration |
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Definition
These two specific substrate concentrations are included in surface dilution kinetics. |
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Term
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Definition
To alter the surface concentration of a substrate, add or remove this from the mixed micelles. |
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Term
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Definition
This does not interfere with catalytic or modulator sites on an enzyme (No change in size, area occupied, and surface charge.) |
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Term
1. Soluble enzyme (E) combines with mixed micelle (A) forms EA 2. If E binds non-specifically to the micelle surface, A is equal to the sum molar concentration of Triton and lipid substrate |
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Definition
Define the terms of the "surface binding model" |
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Term
When enzyme bonds specifically to A, A is equal to the molar concentration of lipid substrate |
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Definition
Define the "phospholipid binding model" |
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Term
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Definition
Once an enzyme is associated with the Triton, lipid, and mixed micelle, it binds to the individual lipid molecule forming this complex. |
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Term
Mole fraction or mole percentage |
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Definition
The concentration of lipids in a mixed micelle can be shown as... |
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Term
Non-competitive Inhibition |
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Definition
This occurs when the inhibitor binds away from the active site on E or ES |
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Term
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Definition
Occurs when the inhibitor will only bind to the ES complex |
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Term
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Definition
This plots as a parallel line |
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Term
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Definition
The inhibitor combines with and destroys a functional group in the active site of an enzyme |
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Term
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Definition
These become reactive after binding to active site |
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Term
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Definition
The reaction product of one enzyme reaction becomes the substrate for the next |
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Term
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Definition
Function through reversible, non-covalent binding of a modulator molecule |
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Term
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Definition
Occurs when end product inhibits enzyme; slows production |
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Term
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Definition
Most common covalent modification |
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Term
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Definition
How does a phosphate group get added? |
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Term
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Definition
How do you remove phosphate? |
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