Help
Options
Didn't know it?
click below
click below
Knew it?
click below
click below
Don't Know
Remaining cards (0)
Know
retry
shuffle
restart
0:00
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.
Normal Size Small Size show me how
Normal Size Small Size show me how
Enzyme Review 1
BEAR program Exam Prep
| Factors | Characteristics |
|---|---|
| Double-Rciprocal plot | Lineweaver Burk (L-B) Plot 1/V on y-axis 1/[S] on x-axis |
| Holoenzyme | cofactor+enzyme |
| Apoenzyme | protein part of Holoenzyme |
| Non protein co-factor | metal ions (example Ze+, Fe+) |
| Coenzymes | Small organic molecules often derivatives of vitamins |
| Endergonic Reaction | Needs energy to proceed; free energy is positive |
| Exergonic Reaction | Energy is released; free energy is negative |
| Reaction Rate | Number of subtrate molecules converted per unit of time Directly proportional to enzyme concentration at all [S] |
| [S]< Km | Velocity is directly proportional [S], first order, dependant on [S] |
| [S]>Km | velosity is constant, equal to Vmax,independant of [S], Zero order |
| Big Km | high concentration of substrate needed to 1/2 saturate enzyme, low affinity |
| Small Km | low concentration of substance needed to 1/2 saturate enzyme; high affinity |
| Km | substrate concentration at 1/2 Vmax |
| Vmax | saturation of all available binding sites on the enzyme molecules |
| Competative Inhibition | Binds substrate reversibly, Vmax doesn't change, Km increases, L-B plot y-intercept the same |
| 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 |
| Six major classes | Oxidoreductase, Transferase, Hydrolase, Lyase, Isomerase, Ligase |
| Systemic Enzyme Naming | Name of substrate (more than one use colon) followed by action performed + ase |
| Regulating enzyme number | gene expression, covelent modification of proenzymes, proteolytic activity |
| Denature Enzyme | Extreme pH or temperature |
| 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 |
| Kinase | phosphorylates- adds a phosphate group to- proteins (+P) |
| Phosphotase | dephosphorylates- removes a phosphate group from- protiens (-P) |
| Equilibrium | delta G is 0 |
| Michaelis-Menten Equation (M-M eq) | V = (Vmax[S])/(Km+[S]) |
| Lineweaver-Burk Equation(L-B eq) | (1/V)=(Km/Vmax[S]) +(1/Vmax[S]) |
| y = mx + b | (x,y) points on graph. b = y-intercept. m= slope. In L-B plot m= (Km/Vmax) |
| Ribozymes | RNA's that act as enzymes |
| Homotropic Effector | when substrate serves as effector |
| Heterotropic effector | when effector differs from substrate |
| Allosteric Enzyme | Binds substrate + small, physiologically important molecule that can alter activity; composed of multiple subunits |
| Effector | Molecules that bind non-covalently at a site other than the active site; Can alter the Km and/or Vmax |
| Positive and negative effectors | Positive- increases enzyme activity; Negative- decreases enzyme activity |
| Isozyme (Isoenzyme) | catalyze same reaction but have different physical properties due to genetically different amnio acid sequences |
| zymogen | inactive precursors of enzymes involved in blood coagulation |
| 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) |
| 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 |
| Oxidoreductase | catalyzes oxidation-reduction reactions where hydrogen, oxygen or electrons are transferred between molecules |
| Transferases | transfers atoms or groups of atoms/molecules |
| Hydrolases | cleaves bonds by adding water |
| Lyases | elimination reaction; removes group(s) of atoms |
| Isomerases | catalyzes interconversion of isomers (isomers- same chemical formula, different structure) |
| Ligases | catalyzes formation fo bonds and hydrolysis of high energy phosphates |
| Plasma | fluid, non-cellular part of blood |
| Serum | result of centrifuged, coagulated blood |
Created by:
BEARclass
Popular Biology sets