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LCCW Bio1 Final

Biochem Final

Cofactors= ? Things like Metal ions
Coenzymes = ? Small organic groups that are only transiently associated with the enzyme
Prosthetic groups= ? organic groups that are permanently associated with the enzyme
What reactions occur in the mitochondria? TCA cycle, FA oxidation, and oxidation of pyruvate
What reactions occur in the cytosol? Glycolysis, Pentose phosphate pathway and FA biosynthesis
What reactions occur in the Nucleus? DNA and RNA synthesis
What reactions occur in the Lysosome? Degardation of complex macromolecules
What reactions occur in the peroxisomes? additional FA oxidation and detoxification of peroxides occur
Sum up what an enzyme does: The enzyme lowers the energy barrier. It does NOT change the equilibrium constant of a reaction, but it does speed the reaction towards equilibrium (slide #6)
what is Velocity of an enzyme? The rate of product formation per unit of time
According to The Rate Law/Effect of Concentration on reaction rate, if N = 0, then what? Then the reaction proceeds at a rate independent of the concentration of the reactant.
According to The Rate Law/Effect of concentration on reaction rate, if N=1, then what? Then the reaction proceeds at a rate directly proportional to the concentration of the reactant
According to the rate law/Effect of concentration on reaction rate, If N=2, then what? Then the reaction proceeds at a rate proportional to the SQUARE of the concentration of the reactant.
What effects enzymes? Substrate concentration, PH, and Temp
What enzymes exhibit Michaelis-Menton Kinetics? Enzymes that show a hyperbolic curve in response to substrate concentration
What enzymes are said to be allosteric enzymes? Enzymes that show a sigmoid curve in response to substrate concentration
What is the optimal temp range for enzymes in humans? 37C
where can you find Thermophilic bacteria? hot springs (their proteins do not denature until they are very hot
At substrate concentrations well below the Km of an enzyme, describe the rate of reaction = The reaction is 1st order and therefore proceeds at a rate DIRECTLY DEPENDENT of the substrate concentration
At substrate concentrations well above the Km of an enzyme, describe the rate of reaction = The reaction is 0 order and therefore proceeds at a rate related to the square of the substrate concentration
How does Temperature affect most enzymes? Increasing temp speeds up enzyme reactions to a certain point, but too much increase will denature the enzyme. basically
At what PH would you find Pepsin? (in stomach = Acidic) 1.5
At what PH would you find Trypsin? Around 5.5
At what PH would you find Alkaline Phosphatase? Basic - around PH 9
What are the 4 modes of enzyme inhibition? Mixed, Competitive, uncompetitive, and noncompetitive
A competitive inhibitor will have what effect on a target enzyme? Increases Km, does not affect Vmax
What are the 3 assumptions with M-M kinetics model? (1) [S] >>> than the total [ENZYME] (2) The reaction is at steady state (3) The Initial velocities are used to analyze the enzyme
The catalytic efficiency of an enzyme is reflected how? In the kcat value which is equal to the Vmax divided by the total enzyme concentration
In M-M kinetics, Km is equal to what? Equal to the substrate concentration at which the enzyme is at 1/2 Vmax
At a low Km, the enzyme has ______ affinity for the substrate High
At High Km, the enzyme has _____ affinity for the substrate Low
On a Lineweaver-Burke plot of enzyme kinetics date, which value provides the Km? The negative inverse of the X-intercept
On a Lineweaver-Burke plot of enzyme kinetics date, which value provides the Vmax? The y-intercept
Competitive Inhibition occurs how? Occurs when the inhibitor binds at the active site in place of the endogenous substrate
What happens to Vmax and Km in Competitive Inhibition? Vmax remains the same, Km goes up
Non competitive Inhibition occurs how? This type of inhibitor doesn't bind at the active site, but instead binds at an allosteric site away from the active site. It binds to the enzyme in the presence and absence of the native substrate
What happens to Vmax and Km in Noncompetitive Inhibition? Vmax of the enzyme decreases, Km is not affected (because the noncompetitive inhibitor does not interfere with the binding of the substrate)
Enzyme Regulation includes what? Positive regulation, activation, as well as inhibition
Allosteric Mechanisms are what? Mechanisms where the site of the effector binding is away from the active site of the enzyme. The allosteric site is distincy from the active site.
Allosteric can be Positive/negative/both? Both. They can also modify an enzymes Km/Vmax
Allosteric enzymes show what kind of curve? Sigmoidal kinetics/curve
Homotropic effectors are what? Are the substrate of the enzyme acting as the regulatory molecule. These effectors are most often positive effectors so binding is cooperative. (O2 and Hb)
Heterotropic effectors are what? Are effectors that are different than the substrate. The best example of this is a sceme known as feedback inhibition, where the product of an enzyme (metabolic) pathway feeds back to inhibit an earlier step in the pathway.
What is FEEDBACK INHIBITION? It is where the product of an metabolic pathway feeds back to inhibit an earlier step in the pathway
Phosphorylation/De-phosphorylation occurs predominantly at what 3 AA? Ser, Thr and Tyr residues
A noncompetitive inhibitor will bind where on a protein? At an allosteric site
Proteins can be activated by phosphorylation, such as what? Glycogen Phosphorylase
Proteins can be inactivated by phosphorylation, such as what? Glycogen Synthesise
Vitamin B3 is used to Synthesize which cofactor? Nicotinamide Adenine Dinucleotide (NADH/NAD+)
Vitamin B2 is used to synthesize which cofactor? Flavin Mononucleotide (FAD/FADH2/FMN/FMNH2)
Vitamin B1 is used to synthesize which cofactor? Thiamine Pyrophosphate (TPP)
Vitamin B5 is used to synthesize which cofactor? CoASH (coenzyme A)
Vitamin B6 is used to synthesize which cofactor? Pyridoxal Phosphate
Vitamin B9 is used to synthesize which cofactor? Tetrahydrofolate (THF)
Vitamin B12 is used to synthesize which cofactor? Cobalamin
Vitamin H is used to synthesize which cofactor? Biotin
Vitamin C is used to synthesize which cofactor? Ascorbic Acid
Another Name for Vit B1 Thiamine
Another Name for Vit B2 Riboflavin
Another Name for Vit B3 Niacin
Another Name for Vit B5 CoASH
Another Name for Vit B6 Pyridoxine
Another name for Vit B9 Folic Acid
Another name for Vit B12 Cobalamin
Deficiency in Vit B3 = Pellagra (diarrhea, dermatitis, dementia)
Deficiency in Vit B2 = Cheilosis (cracking at the corner of the lips, scaling of the lips)
Deficiency in Vit B1 = Beri Beri and Spina Bifida
Deficiency in Vit B5 = Unknown?
Deficiency in Vit B6 = Peripheral Neuropathy
Deficiency in Vit B9 = Magaloblastic Anemia and neural tube defects
Deficiency in Vit B12 = Pernicious Anemia and Folate Trap
Deficiency in Vit H = Only happens when eating too many raw eggs
Deficiency in Vit C = Scurvy
GLUT-1 = abundant in erythrocytes and at the blood/brain barrier. GLUCOSE UPTAKE
GLUT-2 = In liver, kidney, and beta cells of the pancreas. GLUCOSE IN OR OUT OF CELLS
GLUT-3 = Is the primary transporter in neurons. GLUCOSE UPTAKE
Which GLUT's are primarily involved in glucose UPTAKE? GLUT 1/3/4
Which GLUT's are primarily involved in transporting glucose either into/out of cells depending on need of the organism? GLUT-2 (ONLY)
Why are the enzymes in the plasma often used as diagnostics? The can signal tissue damage, they can mark a change in metabolism, they can serve as a marker of a congenital defect.
THE GLUT transporters are examples of what kind of transporter? Uniport
In glycolysis, where is ATP consumed? Steps 1 and 3
In glycolysis, where is ATP regenerated? Steps 7 and 10
Net total of ATP per Glucose in Glycolysis? 2
Glucokinase vs Hexokinases for Km? Glucokinase has a much higher Km than other hexokinases with a high Vmax
Glucokinase vs Hexokinases for M-M kinetics? Hexokinasess DO follow M-M, but Glucokinases DO NOT!! Glucokinases follow sigmoidal kinetics
Glucokinases vs Hexokinases G6P? Glucokinases are NOT inhibited by physiological concentrations of G6P, but Hexokinases ARE inhibited by it.
What enzymes are potential control points (non-reversible) for glycolysis? Hexokinase, Phosphofructokinase-1 (PFK-1), and Pyruvate Kinase -- they have large negative Delta G's
Which small molecule as the GREATEST effect on the direction of flux through PFK-1 and therefore, glycolysis? Fruc, 2-6-BP (activates PFK-1 and deactivates FBP, thus Fru-6Phos can only continue onto Fru-1,6-BP)
Which hormone is responsible for increasing the production of Fructose 2,6 BP? Insulin
Which 2 molecules are interchangable? and which one continues on to furthe Glycolysis? DHAP and Glyceraldehyde-3-Phosphate (GAP). GAP continues on to become interchangable with (2) 1,3-BPG
What are the products of AEROBIC glycolysis of 1 glucose molecule? 2 NADH, 2 ATP, 2 Pyruvate
How are glucokinase and hexokinases the same? They both have specificity for hexose sugars
In the presence of a low concentration of glucose and a high concentration of fructose-6-phsophate, where does glucokinase reside in the cell? Nucleus
What converts ATP to cAMP? Adenylyl Cyclase
GLucose to G6P is catalyzed by what? Hexokinase and MG2++
G6P to F6P is catalyzed by what? Phosphoglucose isomerase (PGI)
F6P to FBP (fructose 1,6-bisphosphate) is catalyzed by what? Phosphofructokinase (PFK) and MG2++
FBP to DHAP/GAP is catalyzed by what? Aldolase
GAP to DHAP (and vis versa) is catalyzed by what? Enediol intermediate (triose phsophate isomerase)
GAP to 1,3-BPG is catalyzed by what? Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
1,3-BPG to 3PG is catalyzed by what? Phosphoglycerate Kinase (PGK) and MG2++
3PG to 2PG is catalyzed by what? Phosphoglycerate mutase (PGM)
2PG to PEP is catalyzed by what? Enolase
PEP to Pyruvate is catalyzed by what? Pyruvate Kinase (PK)
Muscle uses: Hexokinase/Glucokinase/both/neither? Hexokinase
Liver uses: Hexokinase/glucokinase/both/neither? Glucokinase (which is specific for glucose and doesn't phosphorylate fructose)
What are the 5 coenzymes for pyruvate dehydrogenase complex? CoA, NAD+, FAD+, Lipoic Acid (lipoamide), and TPP
What are the 3 fates of Pyruvate in humans? Lactate, CO2 + H20, and Alanine + Glucose
Which molecules regulate Citrate Synthase? Citrate, NADH/NADH+, Succunyl-CoA
1 complete round of Krebs Cycle yields what? 2 CO2, 3 NADH, 1 FADH2, 1 GTP/ATP
Which ones are HIGH energy molecules? ATP, Acetyl-CoA, NADH, Glucose
Which ones are LOW energy molecules? ADP, AMP, Pyruvate, NAD+, CA+
The total net synthesis of ATP from 1 molecule of glucose is? ~38 under aerobic conditions.
NADH = _____ ATP 3 ATP
FADH = ____ ATP 2 ATP
Which 3 enzymes are likely to function far from equilibrium under physiological conditions? Citrate Synthase, Isocitrate dehydrogenase, Alpha-ketaglutarate dehydrogenase
The C4 epimer of Alph-D-glucopyronose is ___? Alpha-D Mannose
Which AA are hydrophobic? GLY, ALA, VAL, LEU, ILE, MET, PRO, PHE, TYP
List the FA in order from HIGHEST MP to LOWEST MP: HIGHEST (long single bonded chain): Arachadonic>Steric>Palmic Acid >> (double bonds) Oleic > Linolecic > Alpha-linoleic > Arachidonic (4 double bonds)
Proline net charge at pH7? 0
Glutamate net charge at PH 1 and pH 10? pH 1 = +1 // pH 10 = -2
Lysine net charge at pH 1 and pH 10? pH 1 = +2 // pH 10 = -1
Alanine net charge at pH 1 and pH 10? ph 1 = +1 // pH 10 = -1
What are some characteristics of DNA? Right handed, 5'->3', Double stranded, structurally flexible
Which of the following reactions is NOT anaplerotic with respect to the Citric Acid Cycle? FA biosynthesis (ones that ARE anaplerotic = AA catabolism, Pyruvate carbaxylase, and pyruvate dehydrogenase)
What is the net yield of ATP from electron transport/oxidative phosphorylation of NADH? 3
What is the terminal electron acceptor of electron transport? Oxygen
Which of the following bonds has the highest and lowest potential energy? covalent bonds(highest) and London dispersion (weakest)
According to Henderson-Hasselbalch equation, when the pH of a solution of a weak acid is greater than the pKa,.... The Concentration of the conjucant BASE is greater than the ACID
The Anomeric carbon of Alpha-D-Fructofuranose is________? C2 (fructofuranOSE = Ketose = C2 has main branch)
In 0-order reaction, the rate of product formation is = ? Independent of the concentration of the reactant
A reaction with __ delta H and ___ delta S will be NONspontaeous at all temps + and -
A reaction with ___ delta H and _____ delta S will be SPONTANEOUS at all temps - and +
A reaction with ___ delta H and _____ delta S will be SPONTANEOUS at temps ABOVE T= DeltaH/DeltaS + and+
Which combinations of AA will for a salt bridge? ARG and ASP
Function of Co Q? Energy transduction
Function of Retinol? (Vit A) = Antioxidant and Vision
Function of Vit K? Blood clotting
Function of Vit E? Antioxidant
2,3-Bisphosphoglycerate does which of the following? Stabalizes T-state of Hb
What describes how O2 binds to Hb? Cooperatively
An enzyme prosthetic group is defined as: An organic group that permanently associated with an enzyme
Lyases = ? Catalyze cleavage of C-C, C-S and C-N bonds
Oxidoreductases = ? Catalyzes oxidation-reduction reactions
Transferases = ? Catalyze transfer of C/N/or P containing groups
Hydrolases = ? Catalyze cleavage of bonds by adding water
Isomerases = ? Catalyze racemization of optical or geometric isomers
Ligases = ? Catalyze formation of bonds between C and O/S/ and N coupled to hydrolysis of High energy phosphates
What are the 5 ALDOSE'S we need to know? Glyceraldehyde, Ribose, Glucose, Mannose, Galatose
What are the 2(3?) Ketoses we need to know? Dihydroxyacetone (Ribulose), and Fructose
HemiACETAL = ? Alcohol +Aldehyde
HemiKETAL = ? Alcohol + Ketone
Sucrose is made up from what? alpha D Glu + Beta D Fructose
Maltose is made up from what? Alpha-(1-4) Glu + Alpha-(1-4) Glu
IsoMaltose is made up from what? Alpha (1-6) Glu + Alpha (1-6) Glu
Lactose is made up from what? Beta (1-4) Gal, Glu
Cellibiose is made up from what? Beta (1-4) Glu
How are Amylopectin and Glycogen related? Due to branching
Amylopectin branching at what point? 28th point
Glycogen branching at what point? 14th point
Hyluronate is found where? in eyes, synovial fluid, viterous humor
Chondroitin is found where? In Cartilage
Dermatin Sulfate is found where? in wound healing
Keratin Sulfate is found where? Found throughout the body
Heparin is found where? In blood clotting
Oxidation of what carbon in Alpha-D=GLucopyranose yeilds Glucuronic Acid? C6
Reduction of what carbon in D-Ribose yeilds D-Ribitol? C1
What are the 9 essencial AA? HIS, MET, VAL, LEU, ISO, PHE, TYR, THR, LYS
Base skeleton for all sphingolipids? Sphingosine
What are the 5 main hormones we need to know? Cortisol, Aldesterone, Testosterone, Beta Estradiol, Progesteron
Cortisol is in charge of what? Regulating Metabolism
Aldesterone is in charge of what? Regulating salt/water excretion from kidneys
Progesteron is in charge of what? Pregnancy
What is at C1 position in a glycerolphospholipid? C-16 SATURATED FA (Saturated = no double bonds)
What is at C2 position in a glycerolphospholipid? C-20 UNSATURATED FA (unsaturated = Double bonds)
What is at C3 position in a glycerolphospholipid? Phosphate group
Created by: walkingbyfaith09



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