Busy. Please wait.

show password
Forgot Password?

Don't have an account?  Sign up 

Username is available taken
show password


Make sure to remember your password. If you forget it there is no way for StudyStack to send you a reset link. You would need to create a new account.
We do not share your email address with others. It is only used to allow you to reset your password. For details read our Privacy Policy and Terms of Service.

Already a StudyStack user? Log In

Reset Password
Enter the associated with your account, and we'll email you a link to reset your password.
Didn't know it?
click below
Knew it?
click below
Don't know
Remaining cards (0)
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

BC 351- Unit 4

3 steps that are different in gluconeogenesis hexokinase, PFK, pyruvate kinase
hexokinase bypass in gluconeogenesis glucose-6 phosphatase
PFK bypass in gluconeogenesis fructose 1,6 biphosphatase 1
pyruvate kinase bypass in gluconeogenesis pyruvate carboxylase + PEP carboxykinase
Considering the role of ATP formation and hydrolysis in energy coupling of anabolic and catabolic pathways, what must be true? high levels of ATP act as allosteric activators of anabolic pathways
regulation of enzyme activity can affect Km or Vmax or both of the enzyme
heteroallostery second, non substrate effector
In resting muscle cells the regulatory molecule that would accumulate and the enzyme that would be more active are ATP and glycogen synthase
ATP and CTP regulate aspartate transcarbamoylase (ATCase) by binding the R subunit and stabilizing ATCase in the R and T states, respectively.
A mechanism not used by cells to regulate enzyme activities is substrate diffusion rate control.
enzymes have activity in the cell that varies continuously from very high to very low because it is the activity of the population of enzyme molecules that determines the cellular activity
You are studying an enzyme that has a 3-fold increase in KM, but no change in VMax upon phosphorylation... The best interpretation of your result is your enzyme is positively regulated by a protein phosphatase
Regulation of enzyme activity often is found to integrate several types of signals
For ATP hydrolysis, ATP ADP + Pi, what is the effect of changing the reaction conditions from standard chemical conditions to biochemical standard conditions (other than the ATP and ADP concentrations) on ΔG of the reaction? The ΔG of the reaction will be more negative at a given ADP/ATP ratio
catabolic produce ATP & NADH, shut off by high [ATP], activated by low [ATP]
anabolic use ATP and NADH, shut off by low [ATP], activated by high [ATP]
Regulation of metabolic pathways occurs through modulating the activity of paired enzymes catalyzing
Regulation of glycolysis vs. gluconeogenesis is through the response of the key enzymes to indicators of energy charge in the cell like ATP and AMP
The plot of the effect of ATP and AMP on PFK-1 activity indicates ATP is a substrate and inhibitor
F2,6bisP regulates Phosphofructokinase-1 (PFK-1) and Fructose 1,6 BisPhosphatase (F1,6 BisPtse) allosterically (step 3 bypass reactions) *inhibits gluconeogenesis
F2,6bisP is a ____ on PFK-1 heteroallosteric activator
PKA is activated by cAMP (will activate gluconeogenesis)
Regulation of glycolysis and gluconeogenesis in the liver functions to stabilize the glucose levels in the blood through glucagon activation of PKA activity.
When the glucagon concentration in the blood increases the enzymatic activity decreases for PhosphoFructoKinase-2.
each turn of CAC produces 3 NADH, 1 FADH2, 1 GTP
A deficiency in the vitamin thiamine results in higher than normal levels of pyruvate and α- ketoglutarate in the blood suggesting that thiamine is necessary for the function of specific dehydrogenases.
If citrate (C6H8O7) were completely oxidized to CO2 and H2O, the number of molecules of O2 consumed per molecule of citrate would be around A. 2. 5
The reaction of the citric acid cycle that is most similar to the pyruvate dehydrogenase complex-catalyzed conversion of pyruvate to acetyl-CoA is the conversion of α-ketoglutarate to succinyl-CoA.
The reaction of the citric acid cycle that produces an ATP equivalent (in the form of GTP) by substrate level phosphorylation is the conversion of succinyl-CoA to succinate
Anaplerotic reactions produce oxaloacetate and malate to maintain constant levels of citric acid cycle intermediates
The growth of nonphotosynthetic bacteria, but not animal cells, can occur on the carbon source fatty acids
Citrate synthase and the NAD+- specific isocitrate dehydrogenase are two key regulatory enzymes of the citric acid cycle. These enzymes are inhibited by ATP and/or NADH
aerobic respiration arose as an adaptation to increasing levels of oxygen in the atmosphere that had been produced by photosynthesis
matrix pH 8
intermembrane space pH 7
order of ETC 1, 2, Q, 3, Cyt C, 4
complex 1 ETC NADH is used
complex 2 ETC FADH2 is used
ubiquinone/ co Q carries H+ and electrons
cytochromes carry electrons only (redox potential depends on environment)
iron-sulfur proteins carry electrons only (redox potential depends on environment)
mitochondrial electron carriers with the highest redox potential generally contain copper or heme groups
Addition of reduced ubiquinone to mitochondria lacking cytochrome c would not produce a proton gradient because ubiquinone cannot bind to cytochrome c oxidase (C IV) as required to pass electrons to it
The direct generation of a proton gradient by electron-transport proteins requires that the oxidized and reduced states of the electron-transport protein have different conformations.
The coupled redox reaction with enough ΔG to synthesize one molecule of ATP from ADP and Pi under standard conditions is the oxidation of cytochrome c by oxygen
Cotransport of protons from the intermembrane space to the matrix is required for import of acetic acid ions into the matrix from the intermembrane space
The antibiotic bongkrekic acid inhibits the ATP/ADP transport protein across the inner mitochondrial membrane; to allow electron transport to occur in mitochondria treated with bongkrekic acid you can permeabilize the inner membrane to protons
The coupling of electron transport to ATP synthesis is likely to be affected in all of these systems by dinitrophenol (carries protons across membranes)
When the ΔG'° of the ATP synthesis reaction is measured on the surface of the ATP synthase enzyme, it is found to be close to zero. This is thought to be due to stabilization of ATP relative to ADP by enzyme binding
ATP synthase works through conformational changes causing an increase in the affinity for ATP and a decrease in affinity for ADP and Pi
Each complete rotation of the actin filament in ATP synthase requires hydrolysis of 3 ATP
The conversion of 1 mol of fructose 1,6-bisphosphate to 2 mol of pyruvate by the glycolytic pathway results in a net formation of 2 mol of NADH and 4 mol of ATP
During strenuous exercise, the NADH formed in the glyceraldehyde 3-phosphate dehydrogenase reaction in skeletal muscle must be reoxidized to NAD+ if glycolysis is to continue. The most important reaction involved in the reoxidation of NADH is pyruvate → lactate
The anaerobic conversion of 1 mol of glucose to 2 mol of lactate by fermentation is accompanied by a net gain of 2 mol of ATP
Allosteric enzymes usually have more than one polypeptide chain.
Phosphofructokinase-2 and fructose 2,6 bisphosphatase are regulated in their relative activities by phosphorylation by PKA
what is correct regarding the oxidative decarboxylation of pyruvate in aerobic conditions in animal cells? One of the products of the reactions of the pyruvate dehydrogenase complex is a thioester of acetate.
Cells oxidizing acetyl groups through the TCA cycle require molecular oxygen for regeneration of NAD+
Entry of acetyl-CoA into the citric acid cycle is decreased when the ratio of [ATP]/[ADP] is high.
When a glucose molecule is broken down to CO2 in glycolysis and the TCA cycle, little ATP is directly produced, most of the energy is stored as NADH
In the reoxidation of QH2 by purified ubiquinone-cytochrome c reductase (Complex III) from heart muscle, the overall stoichiometry of the reaction requires 2 mol of cytochrome c per mole of QH2 because cytochrome c is a one-electron acceptor, whereas QH2 is a two-electron donor
The electrochemical gradient produced by the electron transport chain is referred to as proton motive force, pmf, or ΔP
ATP synthase is described as a molecular motor
The mitochondrial ATP synthase uses the energy stored in the proton gradient to drive conformational changes in the F1 component β subunit (ATP synthase)
complex 2 is also an enzyme in CAC
chemiosmotic model proton gradient couples ETC to ATP synthase production of ATP
heteroallosteric enzyme regulation describes the mechanism of feedback inhibition of aspartate transcarbamoylase by CTP
regulation of glycolysis and gluconeogenesis in the liver functions to stabilize glucose levels in blood thru glucagon regulation of PKA activity
Cells oxidizing acetyl groups through the TCA cycle require molecular oxygen for regeneration of NAD+
The electron transport chain functions to couple the transfer of e-s from NADH and FADH2 to O2 to transport H+s out of the matrix against a concentration and charge gradient.
Evidence supporting the chemiosmotic theory is exemplified by a higher MIM internal H+ concentration being sufficient for ATP synthesis
The F0 component of the F0F1-ATP synthase serves as a proton channel
F1 component ATPase/ATP synthase
low blood glucose-> glucagon produced, PKA activated, phosphorylate PFK2/FBP2 (levels lowered), increased gluconeogenesis
what reaction accounts for most oxygen consumption? transfer of electrons from cytochrome c to O2
Created by: melaniebeale



Use these flashcards to help memorize information. Look at the large card and try to recall what is on the other side. Then click the card to flip it. If you knew the answer, click the green Know box. Otherwise, click the red Don't know box.

When you've placed seven or more cards in the Don't know box, click "retry" to try those cards again.

If you've accidentally put the card in the wrong box, just click on the card to take it out of the box.

You can also use your keyboard to move the cards as follows:

If you are logged in to your account, this website will remember which cards you know and don't know so that they are in the same box the next time you log in.

When you need a break, try one of the other activities listed below the flashcards like Matching, Snowman, or Hungry Bug. Although it may feel like you're playing a game, your brain is still making more connections with the information to help you out.

To see how well you know the information, try the Quiz or Test activity.

Pass complete!

"Know" box contains:
Time elapsed:
restart all cards