BEAR program Exam Prep
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each of the black spaces below before clicking
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| Double-Rciprocal plot | Lineweaver Burk (L-B) Plot
1/V on y-axis 1/[S] on x-axis
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| Holoenzyme | cofactor+enzyme
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| Apoenzyme | protein part of Holoenzyme
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| Non protein co-factor | metal ions (example Ze+, Fe+)
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| Coenzymes | Small organic molecules often derivatives of vitamins
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| Endergonic Reaction | Needs energy to proceed; free energy is positive
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| Exergonic Reaction | Energy is released; free energy is negative
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| Reaction Rate | Number of subtrate molecules converted per unit of time
Directly proportional to enzyme concentration at all [S]
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| [S]< Km | Velocity is directly proportional [S], first order, dependant on [S]
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| [S]>Km | velosity is constant, equal to Vmax,independant of [S], Zero order
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| Big Km | high concentration of substrate needed to 1/2 saturate enzyme, low affinity
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| Small Km | low concentration of substance needed to 1/2 saturate enzyme; high affinity
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| Km | substrate concentration at 1/2 Vmax
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| Vmax | saturation of all available binding sites on the enzyme molecules
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| Competative Inhibition | Binds substrate reversibly, Vmax doesn't change, Km increases, L-B plot y-intercept the same
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| Non-competative Inhibition | binds different site on enzyme than substrate; can bind E or ES, Vmax Decreases, No change in Km, L-B plot same x-intercept
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| Six major classes | Oxidoreductase, Transferase, Hydrolase, Lyase, Isomerase, Ligase
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| Systemic Enzyme Naming | Name of substrate (more than one use colon) followed by action performed + ase
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| Regulating enzyme number | gene expression, covelent modification of proenzymes, proteolytic activity
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| Denature Enzyme | Extreme pH or temperature
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| Active Site | special pocket or cleft that creats 3-# surface complementary to substrate, chemical facilitation of substrate to product via stabilizing transition state and catalytic groups
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| Kinase | phosphorylates- adds a phosphate group to- proteins (+P)
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| Phosphotase | dephosphorylates- removes a phosphate group from- protiens (-P)
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| Equilibrium | delta G is 0
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| Michaelis-Menten Equation (M-M eq) | V = (Vmax[S])/(Km+[S])
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| Lineweaver-Burk Equation(L-B eq) | (1/V)=(Km/Vmax[S]) +(1/Vmax[S])
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| y = mx + b | (x,y) points on graph. b = y-intercept. m= slope. In L-B plot m= (Km/Vmax)
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| Ribozymes | RNA's that act as enzymes
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| Homotropic Effector | when substrate serves as effector
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| Heterotropic effector | when effector differs from substrate
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| Allosteric Enzyme | Binds substrate + small, physiologically important molecule that can alter activity; composed of multiple subunits
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| Effector | Molecules that bind non-covalently at a site other than the active site; Can alter the Km and/or Vmax
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| Positive and negative effectors | Positive- increases enzyme activity; Negative- decreases enzyme activity
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| Isozyme (Isoenzyme) | catalyze same reaction but have different physical properties due to genetically different amnio acid sequences
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| zymogen | inactive precursors of enzymes involved in blood coagulation
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| Enzyme | Protein catalyst that increases the rate of reaction without being changed in the process; high specificity and catalytic efficiency (lowers activation energy of a reaction)
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| Free Energy | energy associated with a chemcial reaction that can be used to do work; change in free energy predicts which direction a reaction will spontaneously proceed
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| Oxidoreductase | catalyzes oxidation-reduction reactions where hydrogen, oxygen or electrons are transferred between molecules
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| Transferases | transfers atoms or groups of atoms/molecules
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| Hydrolases | cleaves bonds by adding water
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| Lyases | elimination reaction; removes group(s) of atoms
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| Isomerases | catalyzes interconversion of isomers (isomers- same chemical formula, different structure)
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| Ligases | catalyzes formation fo bonds and hydrolysis of high energy phosphates
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| Plasma | fluid, non-cellular part of blood
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| Serum | result of centrifuged, coagulated blood
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