Term
| some things we'll be looking at in Biochem |
|
Definition
-How macromolecules are made and broken down,
-How the structures of macromolecules relates their funcPons,
-How energy and elements (especially carbon, oxygen, and nitrogen) flow
through biological systems,
-How biological reactions are catalyzed, and
-How biological pathways are regulated. |
|
|
Term
| the 4 types of macromolecules in biochem |
|
Definition
-lipids
-proteins
-nucleic acids
-carbohydrates |
|
|
Term
|
Definition
| the chemistry of life processes; life processes thru the lens of chemistry |
|
|
Term
| where most of the focus is in Biochem |
|
Definition
| most of the focus is on the molecules, their structure, and their activity |
|
|
Term
|
Definition
|
|
Term
| water content of a typical cell |
|
Definition
|
|
Term
| the role of water in biochem |
|
Definition
Water is the solvent of life.
• Most biomolecules dissolve in water
• Biological reactions take place in water
• Water participates in essential biological reactions.
• Water is essentially responsible for the remarkable structure and
function of the biomolecules, organelles and cells. |
|
|
Term
| how water affects biomolecules, organelles, and cells |
|
Definition
| Water is essentially responsible for the remarkable structure and function of the biomolecules, organelles and cells. |
|
|
Term
|
Definition
| Transient, non-covalent, chemical interactions |
|
|
Term
| importance of weak interactions |
|
Definition
| they form the basis of biochemistry and life itself |
|
|
Term
| why H bonds occur in water |
|
Definition
| because of water's polarity |
|
|
Term
| this accounts for the cohesiveness of water |
|
Definition
The polarity of water allows the formation of
hydrogen bonds between water molecules |
|
|
Term
| why water can dissolve many important biochemicals |
|
Definition
|
|
Term
| what causes the hydrophobic effect? |
|
Definition
| The inability of water to dissolve nonpolar molecules |
|
|
Term
| some things that can be attributed to the polarity of water |
|
Definition
-formation of H bonds
-cohesiveness of water
ability to dissolve many important biomolecules |
|
|
Term
|
Definition
| an important organizing principle caused by the inability of water to dissolve nonpolar molecules |
|
|
Term
| some of the interactions we'll be studying |
|
Definition
-electrostatic interactions
-H bonds
-van der Waals interactions |
|
|
Term
| ElectrostaPc Interactions |
|
Definition
Interactions between distinct electrical charges on atoms
example: water molecules dissolving NaCl |
|
|
Term
| electrostatic interactions aka... |
|
Definition
-ionic bonds
-salt bridges |
|
|
Term
|
Definition
| Forms between an electronegative atom (e.g., F, O, N) and Hydrogen |
|
|
Term
|
Definition
| seems to be the F, O, or N that's covalently bound to the H |
|
|
Term
|
Definition
| seems to be the F, O, or N that's not covalently bound to that H |
|
|
Term
| depiction of H bond donors and acceptors (might wanna draw this) |
|
Definition
|
|
Term
|
Definition
| when H is covalently bonded to an electronegative atom |
|
|
Term
| how water disrupts hydrogen bonds between two molecules |
|
Definition
by competing for the hydrogen bonding capability
example:
[image] |
|
|
Term
| where van der Waals interactions take place |
|
Definition
| between nonpolar and uncharged molecules |
|
|
Term
| van der Waals interactions take place between ______ and ______ molecules |
|
Definition
|
|
Term
| The basis of the van der Waals interaction |
|
Definition
| transient asymmetry in one molecule will induce complementary asymmetry in a nearby molecule |
|
|
Term
| energy of a van der Waals interaction vs. distance (might wanna draw this) |
|
Definition
|
|
Term
|
Definition
| the measure of randomness for the whole system itself |
|
|
Term
| one reason water doesn't dissolve nonpolar molecules |
|
Definition
| because water has greater entropy if it doesn't dissolve nonpolar molecules |
|
|
Term
| Hydrophobic molecules such as benzene tend to ______ in aqueous soluPons. |
|
Definition
|
|
Term
|
Definition
| the clustering of hydrophobic molecules in water |
|
|
Term
| Second Law of Thermodynamics |
|
Definition
| The total entropy of a system and its surroundings always increases in a spontaneous process. |
|
|
Term
| biological importance of hydrophobic effect |
|
Definition
| Hydrophobic effect is a powerful organizing force in biological systems |
|
|
Term
| membrane formation is powered by... |
|
Definition
|
|
Term
| composition of a phospholipid |
|
Definition
| hydrophilic head and hydrophobic tail |
|
|
Term
| what happens to phospholipids when they are exposed to water? |
|
Definition
|
|
Term
| how the formation of a phospholipid membrane increases entropy |
|
Definition
| by releasing water into the environment, allowing the water to have greater entropy |
|
|
Term
| protein folding is powered by... |
|
Definition
|
|
Term
| which version of protein has less entropy: folded or unfolded? |
|
Definition
|
|
Term
| why the folding of a protein into something ordered happens spontaneously |
|
Definition
| because it is powered by the hydrophobic effect and increases the entropy of the water |
|
|
Term
|
Definition
| H+ concentration of a solution |
|
|
Term
|
Definition
| pH = log(1/[H+]) = -log([H+]) |
|
|
Term
| acid is a proton donor or acceptor? |
|
Definition
|
|
Term
| base is a proton donor or acceptor? |
|
Definition
|
|
Term
| what the proton does in water |
|
Definition
| complexes with water to form hydronium ion |
|
|
Term
| what strong acids do in solution |
|
Definition
|
|
Term
| what weak acids do in solution |
|
Definition
| partially dissociate and establish e'librium |
|
|
Term
| what happens at a'librium? |
|
Definition
| formation of products and reactants happens at the same time at the same rate |
|
|
Term
|
Definition
| The chemical formed upon ionization of an acid |
|
|
Term
|
Definition
| the acid formed when a base binds a proton |
|
|
Term
| how to calculate the ionization equilibrium of a weak acid |
|
Definition
|
|
Term
| how to calculate the e'librium constant of a weak acid |
|
Definition
|
|
Term
|
Definition
| pKa = log(1/Ka) = -log(Ka) |
|
|
Term
| relationship between pH and pKa (Henderson-Hasselbach equation) |
|
Definition
| pH = pKa + log([A-]/[HA])
A- = conjugate base |
|
|
Term
|
Definition
| the pH at which the acid is half dissociated |
|
|
Term
| the protonated form is the acid or base? |
|
Definition
|
|
Term
| the deprotonated form is the acid or base? |
|
Definition
|
|
Term
|
Definition
| A- (deprotonated form) predominates |
|
|
Term
|
Definition
| HA (protonated form) predominates |
|
|
Term
|
Definition
| An acid-base conjugate pair that resists changes in the pH of a solution |
|
|
Term
| when a buffer is most effective |
|
Definition
| when the pH is near its pKa |
|
|
Term
| what buffers the pH of blood? |
|
Definition
| the conjugate acid-base pair of carbonic acid and bicarbonate (H2CO3/HCO3
-) |
|
|
Term
| the rxn that happens with CO2 in blood |
|
Definition
| CO2 + H2O <--> H2CO3 <--> H+ + HCO3- |
|
|
Term
| electrostatic interaction forms between... |
|
Definition
| distinct electrical charges |
|
|
Term
|
Definition
| an electronegative atom and Hydrogen |
|
|
Term
| van der Waals interaction forms between... |
|
Definition
| nonpolar and uncharged molecules due to transient asymmetry in electrical charge |
|
|
Term
| what causes van der Waals forces? |
|
Definition
| dipole-dipole interaction |
|
|
Term
| dipole-dipole interaction |
|
Definition
| interactions of atoms due to transient asymmetry in electrical charge |
|
|
Term
|
Definition
| clustering of hydrophobic molecules in water |
|
|
Term
| The hydrophobic effect is powered by... |
|
Definition
| the increase in the entropy of water that results when hydrophobic molecules come together. |
|
|
Term
| Protein folding is powered by... |
|
Definition
|
|
Term
| use of weak interactions in proteins |
|
Definition
| used to stabilize 3D structure |
|
|
Term
| depiction of how an amino acid changes in response to pH |
|
Definition
|
|
Term
| depiction of how peptide bonds are formed |
|
Definition
|
|
Term
| this is considered the beginning of the polypeptide chain |
|
Definition
|
|
Term
| this is considered the end of the polypeptide chain |
|
Definition
|
|
Term
| the only covalent rxn that can happen in a protein other than formation of peptide bonds |
|
Definition
| formation of disulfide bridge |
|
|
Term
| depiction of how a disulfide bridge is formed |
|
Definition
|
|
Term
| the resonance that occurs in a peptide bond |
|
Definition
|
|
Term
| distance between R groups in energetically favorable form |
|
Definition
| energetically favorable form has R groups far from each other |
|
|
Term
| configuration of most peptide bonds |
|
Definition
|
|
Term
| why most peptide bonds are in trans conformation |
|
Definition
| to minimize steric clashes between R groups |
|
|
Term
|
Definition
| the three-dimensional structure formed by hydrogen bonds between pep |
|
|
Term
| some prominent examples of protein secondary structure |
|
Definition
|
|
Term
| the most common secondary structure |
|
Definition
|
|
Term
| where H bonding occurs in the α-helix |
|
Definition
| it's always 4 amino acids ahead |
|
|
Term
| some things that determine likelihood of an amino acid being in an α-helix |
|
Definition
-crowding on the beta C
-distance of H bonding O from backbone |
|
|
Term
| Beta sheets are formed by... |
|
Definition
|
|
Term
| some ways beta sheets can be aligned |
|
Definition
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
| how polypeptides are stabilized in secondary structure |
|
Definition
| by H bonding in the backbone |
|
|
Term
|
Definition
| just the sequence thru peptide bonds |
|
|
Term
|
Definition
| the result of H bonding along the backbone |
|
|
Term
|
Definition
| the result of the protein folding into its structure |
|
|
Term
| what determines the structure a protein folds into? |
|
Definition
|
|
Term
| formation of tertiary structure is powered by... |
|
Definition
|
|
Term
| interactions that occur between hydrophobic molecules within a protein |
|
Definition
| van der Waals interactions |
|
|
Term
|
Definition
| multiple polypeptide chains called subunits |
|
|
Term
| depiction of how electrophoresis separates mixtures of molecules |
|
Definition
|
|
Term
|
Definition
|
|
Term
| how much enzymes speed up rxns |
|
Definition
|
|
Term
| the an- in anhydrase means... |
|
Definition
|
|
Term
|
Definition
| breaking of a bond by addition of a water molecule |
|
|
Term
|
Definition
|
|
Term
|
Definition
| catalyze the hydrolysis of peptide bonds |
|
|
Term
| are all enzymes equally specific? |
|
Definition
|
|
Term
| the 6 major classes of enzymes |
|
Definition
-Oxidoreductase
-Transferases
-Hydrolyases
-Lyases
-Isomerases
-Ligases |
|
|
Term
|
Definition
| catalyze oxidation-reduction reactions |
|
|
Term
|
Definition
| move functional groups between molecules |
|
|
Term
|
Definition
| cleave bonds with the addition of water |
|
|
Term
|
Definition
| remove atoms to form double bonds or add atoms to double bonds |
|
|
Term
|
Definition
move functional groups within a molecule
converts molecule to another isomer |
|
|
Term
|
Definition
| join two molecules at the expense of ATP |
|
|
Term
|
Definition
a measure of energy capable of doing work
this is the energy within the bonds of a molecule that is capable of doing work |
|
|
Term
| do enzymes alter the ΔG of a reaction? |
|
Definition
|
|
Term
| when rxn occurs spontaneously |
|
Definition
|
|
Term
|
Definition
|
|
Term
| when rxn does not occur spontaneously |
|
Definition
|
|
Term
|
Definition
|
|
Term
| when rxn is at e'librium,... |
|
Definition
there is no net change in the amount of reactant or product
ΔG = 0 |
|
|
Term
| The ΔG of a reaction depends only on... |
|
Definition
| the free energy difference between reactants and products |
|
|
Term
| does the ΔG of a reaction provide any ΔG of a reaction? |
|
Definition
|
|
Term
| do enzymes alter rxn rate? |
|
Definition
|
|
Term
| do enzymes alter rxn e'librium? |
|
Definition
|
|
Term
| The reaction equilibrium is determined only by... |
|
Definition
| the free energy difference between the products and reactants |
|
|
Term
|
Definition
| a molecular form that is no longer substrate but not yet product |
|
|
Term
|
Definition
| the formation of the transition state |
|
|
Term
|
Definition
| The energy required to form the transition state from the substrate |
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
| how to calculate activation energy |
|
Definition
|
|
Term
| the first step in enzymatic catalysis |
|
Definition
| the formation of an enzyme-substrate complex |
|
|
Term
|
Definition
| region of an enzyme where the enzyme-substrate complex forms |
|
|
Term
| this promotes the formation of the transition state |
|
Definition
| The interaction of the enzyme and substrates at the active site |
|
|
Term
| some common features of active sites of enzymes |
|
Definition
1. The active site is a three-dimensional cleft or crevice created by amino acids from different parts of the primary structure.
2. The active site constitutes a small portion of the enzyme volume.
3. Active sites create unique microenvironments.
4. The interaction of the enzyme and substrate at the active site involves multiple weak interactions.
5. Enzyme specificity depends on the molecular architecture at the active site. |
|
|
Term
| structure of the active site |
|
Definition
| a three-dimensional cleft or crevice created by amino acids from different parts of the primary structure |
|
|
Term
| how much of the enzyme is taken up by the active site? |
|
Definition
|
|
Term
|
Definition
|
|
Term
| The interaction of the enzyme and substrate at the active site involves... |
|
Definition
| multiple weak interactions |
|
|
Term
| Enzyme specificity depends on... |
|
Definition
| the molecular architecture at the active site |
|
|
Term
| do enzymes follow the lock-and-key model? |
|
Definition
|
|
Term
| what model do enzymes almost always follow? |
|
Definition
|
|
Term
|
Definition
| the enzyme changing shape upon substrate binding |
|
|
Term
|
Definition
| the free energy released upon interaction of the enzyme and substrate |
|
|
Term
| Binding energy is greatest when... |
|
Definition
| the enzyme interacts with the transition state |
|
|
Term
| what facilitates the formation of a transition state when an enzyme is involved? |
|
Definition
|
|
Term
| important characteristic of an enzyme inhibitor |
|
Definition
| has to resemble the transition state |
|
|
Term
| how to calculate binding energy |
|
Definition
| binding energy = uncatalyzed activation energy - catalyzed activation energy |
|
|
Term
| which amino acids would you expect to be on the outside of an alpha-helix in a plasma membrane? |
|
Definition
| hydrophobic/nonpolar amino acids |
|
|
Term
| which amino acids would you expect to be on the inside of an alpha-helix in a plasma membrane? |
|
Definition
| polar/hydrophilic amino acids |
|
|
Term
| What reaction does CA catalyze? |
|
Definition
|
|
Term
|
Definition
|
|
Term
| how water complexes with the Zn ion in carbonic anhydrase |
|
Definition
| -Zn2+ acts as a Lewis acid
-water then compensates for loss of electrons by releasing a proton |
|
|
Term
| how a water molecule compensates for loss of electrons |
|
Definition
|
|
Term
| why the pKa of water is 15.7 |
|
Definition
| because for every 55.5 mols of water, there's 10-7 mols of H+ and 10-7 mols of OH-
therefore,...
Ka = (10-7 X 10-7) / 55.5 = 1.8 X 10-16
therefore,...
pKa = -log (1.8 X 10-16) = 15.7 |
|
|
Term
| depiction of how carbonic anhydrase reacts with water |
|
Definition
|
|
Term
|
Definition
|
|
Term
| some reasons tyrosine replacing a histidine can affect the function of CA |
|
Definition
-at physiological pH, histidine can be protonated or deprotonated, but tyrosine can only be protonated
-histidine can make 2 H bonds while tyrosine can make only one H bond |
|
|
Term
| why tyrosine is not a good AA for the active site of CA |
|
Definition
| -Does not interact with H2O or OH-
-Does not interact with Zn2+
-Slower rate of catalysis |
|
|
Term
|
Definition
| Bone cells that break down and remove bone Issue – dissolve the fibers and matrix of bone |
|
|
Term
|
Definition
| breaking bonds by addition of water |
|
|
Term
| why is initial velocity (V0) used in measuring catalysis? |
|
Definition
| because you're interested in the initial product formation |
|
|
Term
| the kinetics of Michaelis-Menten enzymes |
|
Definition
| starts off first order with respect to S, then seems to be zero order with respect to S |
|
|
Term
| when the kinetics of a Michaleis-Menten enzyme become zero-order |
|
Definition
| when all the enzyme is bound to substrate |
|
|
Term
| in this rxn, why do we ignore k2?
[image] |
|
Definition
| Because we examine only the initial rates |
|
|
Term
| quantities of enzymes compared to quantities of substrates |
|
Definition
| enzymes are almost always in way less quantities than substrates |
|
|
Term
| how calculate V0 (initial velocity) (the Michaelis-Menten equation) |
|
Definition
| V0 = (Vmax[S]) / (KM + [S])
this is the Michaelis-Menten equation |
|
|
Term
| how to calculate KM (the Michaelis-Menten constant) |
|
Definition
| KM = (k-1 + k2) / k1 = (ES falls apart) / (ES forms)
here's a depiction of it:
[image] |
|
|
Term
| KM is an indication of... |
|
Definition
| -the stability of the [ES] complex
-Tells how much substrate will saturate E (~10 × KM) |
|
|
Term
| KM vs. enzyme affinity for substrate |
|
Definition
|
|
Term
|
Definition
| Vmax = k2 X [E]Total
or
Vmax = kcat X [E]Total
k2 is a constant |
|
|
Term
|
Definition
|
|
Term
|
Definition
| k2 or kcat = Vmax / [E]Total |
|
|
Term
| in Michaelis-Menten Kinetics, what happens when you change [E]? |
|
Definition
| k2 or kcat doesn't change, but Vmax does |
|
|
Term
|
Definition
| the rate constant of the rate-limiting step |
|
|
Term
| relationship between k2 and kcat |
|
Definition
|
|
Term
|
Definition
| The number of molecules of substrate converted per unit time per enzyme molecule |
|
|
Term
| kcat/KM is a measure of... |
|
Definition
|
|
Term
|
Definition
|
|
Term
|
Definition
| How fast the ES makes product |
|
|
Term
|
Definition
|
|
Term
| relationship between kcat and KM |
|
Definition
| kcat/KM = (How fast the ES makes product)/(How easily ES is formed) |
|
|
Term
| for an enzyme to be highly efficient, you want kcat to be ______ and KM to be ______ |
|
Definition
|
|
Term
| for an enzyme to be highly efficient, you want ______ to be high and ______ to be low |
|
Definition
|
|
Term
| is Vmax estimated or measured? |
|
Definition
|
|
Term
| the Lineweaver-Burk equation |
|
Definition
| (1/V0) = ((KM/Vmax) X (1/[S])) + (1/Vmax)
y = ax + b
y = 1/V0
a = KM/Vmax
x = 1/[S]
b = 1/Vmax |
|
|
Term
| value of kcat/KM vs. enzyme efficiency |
|
Definition
|
|
Term
| enzymes that do not follow standard Michaelis-Menten kinetics |
|
Definition
| allosteric enzymes/proteins |
|
|
Term
| allosteric enzymes/proteins |
|
Definition
| enzymes that “switch” between functioning and non-functioning (or more and less active) conformations |
|
|
Term
| how allosteric enzymes/proteins are regulated |
|
Definition
-Binding of a regulator at a site distant from the active site
-Cooperative binding of multiple substrate molecules
-Or both |
|
|
Term
| regulators of allosteric enzymes/proteins |
|
Definition
molecules that bind at a site distant from the active site to regulate the activity of the enzyme
they are inhibitors and activators |
|
|
Term
| how regulators affect allosteric enzymes/proteins |
|
Definition
| they induce changes in 4° structure |
|
|
Term
| the structure allosteric enzymes/proteins have |
|
Definition
|
|
Term
| a step in metabolic pathways that's always regulated by allosteric enzymes |
|
Definition
|
|
Term
|
Definition
| end product binding to regulatory site on allosteric enzyme distinct from active site |
|
|
Term
| the enzymes that facilitate steps in biochemical pathways other than the committed step |
|
Definition
|
|
Term
| composition of hemoglobin |
|
Definition
| 4 O2 binding subunits: 2 α and 2β (pair of identical αβ dimers) |
|
|
Term
| how O bonding affects the structure of hemoglobin |
|
Definition
| Binds O2 cooperatively: as one subunit binds O2, Hb conformation changes, increasing O2 affinity of other subunits |
|
|
Term
| how the structure of myoglobin differs from that of hemoglobin |
|
Definition
| hemoglobin has 4 polypeptide chains while myoglobin has only 1 |
|
|
Term
| behavior of myoglobin compared to that of hemoglobin |
|
Definition
| hemoglobin behaves like an allosteric enzyme while myoglobin behaves like a Michaelis-Menten enzyme |
|
|
Term
| where hemoglobin takes up O |
|
Definition
|
|
Term
| where hemoglobin releases O |
|
Definition
|
|
Term
| when hemoglobin has low affinity for O |
|
Definition
| when there's no O bound to it |
|
|
Term
| T state of hemoglobin is favored until... |
|
Definition
| O has bound to one subunit of each αβ dimer |
|
|
Term
| R state of hemoglobin is favored until... |
|
Definition
| O is released from one complete αβ dimer |
|
|
Term
| what O does to the Fe atom in hemoglobin when O bonds to hemoglobin |
|
Definition
|
|
Term
| the 2 oxidation states of Fe |
|
Definition
|
|
Term
| depiction of how O bonding to hemoglobin alters the structure of the molecule |
|
Definition
[image]
this induces conformational changes in one Hb chain, which triggers a conformational change in other Hb chains |
|
|
Term
| the bonds that occur between O and hemoglobin |
|
Definition
-covalent with Fe
-H bond with distal Histidine |
|
|
Term
|
Definition
| decrease in pH or increase in CO2 leads to stabilization of the T state of Hb and unloading of O2 (and the reverse...) |
|
|
Term
| the role of 2,3-Biphosphoglycerate (2,3-BPG) |
|
Definition
| binds to the interior of the hemoglobin to reduce its affinity for O |
|
|
Term
| what CO2 does with amino acid side chains to help hemoglobin release O |
|
Definition
| covalently binds with side chains to form carbamate |
|
|
Term
| depiction of CO2 binding with side chains to form carbamate |
|
Definition
| [image]
this also helps us exhale CO2 |
|
|
Term
| why mutant hemoglobin forms 2 bands in electrophoresis as oppose to normal hemoglobin forming one band |
|
Definition
| people with mutant hemoglobin produce both normal and mutant hemoglobin; the mutant hemoglobin has greater negative charge, making it move faster to the positive end |
|
|
Term
|
Definition
| dissociation over binding |
|
|
Term
| types of gel electrophoresis with proteins |
|
Definition
|
|
Term
| native gel electrophoresis |
|
Definition
| electrophoresis with protein as it occurs naturally in the organism |
|
|
Term
| native gel electrophoresis separates proteins based on... |
|
Definition
|
|
Term
| denatured gel electrophoresis |
|
Definition
| protein gets denatured, often by a salt called SDS that covers protein in negative charge |
|
|
Term
| denatured gel electrophoresis separates proteins based on... |
|
Definition
|
|
Term
| types of bonds that form in reversible enzyme-inhibitor binding |
|
Definition
| mostly electrostatic and weak interactions with the enzyme rather than covalent |
|
|
Term
| types of bonds that form in irreversible enzyme-inhibitor binding |
|
Definition
| mostly covalent bonds with the enzyme rather than electrostatic and weak interactions |
|
|
Term
| equation for enzyme catalysis |
|
Definition
|
|
Term
| mechanism for competitive inhibition |
|
Definition
|
|
Term
| mechanism for uncompetitive inhibition |
|
Definition
|
|
Term
| mechanism for noncompetitive inhibition |
|
Definition
|
|
Term
| what competitive inhibitors bind to |
|
Definition
|
|
Term
| how competitive inhibitors affect the catalysis rxn |
|
Definition
|
|
Term
| what happens wen you add extra substrate when there's a competitive inhibitor? |
|
Definition
| substrate outcompetes comprtitive inhibitor |
|
|
Term
|
Definition
|
|
Term
| how competitive inhibitor affects Vmax |
|
Definition
|
|
Term
|
Definition
when enzyme is saturated with substrate
happens only when there's excess amounts of substrate |
|
|
Term
| how competitive inhibitor affects KM |
|
Definition
|
|
Term
| why competitive inhibitor increases KM |
|
Definition
| because of effectively reduced affinity for enzyme |
|
|
Term
|
Definition
| the [S] at which 1/2 Vmax is reached |
|
|
Term
| what uncompetitive inhibitors bind to |
|
Definition
|
|
Term
| how uncompetitive inhibitors affect the catalysis rxn |
|
Definition
| effectively increases [ES] |
|
|
Term
| how uncompetitive inhibitor affects Vmax |
|
Definition
|
|
Term
| why competitive inhibitor lowers Vmax |
|
Definition
| because of increased [ES] |
|
|
Term
| how uncompetitive inhibitor affects KM |
|
Definition
|
|
Term
| why competitive inhibitor increases KM |
|
Definition
| because of increased [ES] |
|
|
Term
| what noncompetitive inhibitor binds to |
|
Definition
| both enzyme and ES complex |
|
|
Term
| structure of noncompetitive inhibitor |
|
Definition
| not similar to that of substrate |
|
|
Term
| how noncompetitive inhibitor affects catalysis rxn |
|
Definition
| could lower concentrations of E and ES, but proportions of E and ES stay the same |
|
|
Term
|
Definition
| inhibitor that results in unequal proportions of EI and ESI |
|
|
Term
| how noncompetitive inhibitor affects Vmax |
|
Definition
|
|
Term
| how noncompetitive inhibitor affects KM |
|
Definition
|
|
Term
| why KM stays the same when there's a noncompetitive inhibitor |
|
Definition
| same affinity for substrate |
|
|
Term
what inhibitor is this?
[image] |
|
Definition
|
|
Term
what inhibitor is this?
[image] |
|
Definition
|
|
Term
what inhibitor is this?
[image] |
|
Definition
|
|
Term
what inhibitor is this?
[image] |
|
Definition
|
|
Term
what inhibitor is this?
[image] |
|
Definition
|
|
Term
what inhibitor is this?
[image] |
|
Definition
|
|
