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Lecture notes Chapter 27-28
Lecture notes Chapter 27-28

... Consider a tuna sandwich for our example. In stage 1 of metabolism, the processes of digestion break down the large macromolecules into small monomer units. The polysaccharides in bread break down to monosaccharides, the lipids in the mayonnaise break down to glycerol and fatty acids, and the prote ...
Metabolism II
Metabolism II

... Procaryotic ETCs Located in plasma membrane Some resemble mitochondrial ETC, but many are different – different electron carriers – may be branched – may be shorter – may have lower P/O ratio ...
Energy Metabolism - 35-206-202
Energy Metabolism - 35-206-202

... glucose • Illustrate how energy is extracted from glucose, fatty acids, amino acids, and alcohol using metabolic pathways, such as glycolysis, beta oxidation, the citric acid cycle, and the electron transport system • Describe the role that acetyl Co-A plays in cell metabolism ...
2 ATP
2 ATP

... Oxygen breaks Carbon-Carbon bonds Broken bonds release energy & electrons Energy used to form ATP Electrons captured by NAD+ and FAD+ ...
File - SBI
File - SBI

... 8. Why isn't anaerobic respiration effective for larger organisms? a. The energy yield is too small b. It causes too much glucose to be burned up c. It results in products that may be toxic to the organism d. NAD+ is lost over time because it can't be regenerated e. Only d is false 9. More ATP is pr ...
מצגת של PowerPoint - Tel Aviv University
מצגת של PowerPoint - Tel Aviv University

... There are cases in which the green opsin is duplicated on the X chromosome. Red and green are very similar in amino-acid sequence (96%). Blue is more diverged (43%). ...
Citric acid cycle • What are the functions of Citric Acid Cycle?
Citric acid cycle • What are the functions of Citric Acid Cycle?

... The citric acid cycle can be drained of intermediaries The second purpose of the tricarboxylic acid cycle is to provide the cell with building blocks for the biosynthesis of e.g. amino acids , heme and fatty acids. A consequence is that a lack of intermediaries can impair the oxidative function. ...
Document
Document

... pump H+ from the mitochondrial matrix to the intermembrane space. • H+ then moves back across the membrane, passing through the protein, ATP synthase. • ATP synthase uses the exergonic flow of H+ to drive phosphorylation of ATP. • This is an example of chemiosmosis, the use of potential energy in a ...
Notes
Notes

... organic catalyst to speed a chemical reaction. • An enzyme brings together particular molecules and causes them to react. • The reactants in an enzymatic reaction are called the substrates for that enzyme. • For series of reactions below, A is substrate for E1 and B is product. B then becomes substr ...
Chapter 9 Pictures
Chapter 9 Pictures

... March 19. Do it before you leave for spring break. No excuses !!!!! Final Day to drop a class is Friday, March ...
TCA Cycle - eCurriculum
TCA Cycle - eCurriculum

... Catalyzed by succinate dehydrogenase, enzyme directly linked to the electron transport chain.  )G 0 ’= 0. Uses FAD because the free energy change is not enough to generate NADH.  7)  fumarate + H2O  ↔  malate  Catalyzed by fumarase.  )G 0 ’= 0.  8)  malate + NAD +  ↔  oxaloacetate + NADH  Catalyzed  ...
Slide 1
Slide 1

... 6.10 Most ATP production occurs by oxidative phosphorylation  Electrons from NADH and FADH2 travel down the electron transport chain to O2.  Oxygen picks up H+ to form water. ...
`Metabolic flux` describes the rate of flow of intermediates through a
`Metabolic flux` describes the rate of flow of intermediates through a

... The R-state of PFK promotes binding of F6P; the T-state has low affinity for F6P In T-state (blue), charge ...
Water - University of California, Los Angeles
Water - University of California, Los Angeles

... The R-state of PFK promotes binding of F6P; the T-state has low affinity for F6P In T-state (blue), charge ...
lecture2
lecture2

... acid serve as cofactors the mechanism is analogous to that of Pyruvate dehydrogenases. Arsenite is an inhibitor of the enzyme. ...
Chapter 16 solutions
Chapter 16 solutions

... Glycolysis proceeds in the presence of arsenate, but the ATP normally formed in the conversion of 1,3-bisphosphoglycerate into 3-phosphoglycerate is lost. Thus, arsenate uncouples oxidation and phosphorylation by forming a highly labile acyl arsenate. ...
Objectives_Set1
Objectives_Set1

... Draw structures for the gluconeogenic precursors and products identify the enzymes that differ from those of glycolysis. ...
Study Guide
Study Guide

... Name ______________________________ Class ___________________ Date __________________ ...
MedBiochem Exam For each of the following questions, choose the
MedBiochem Exam For each of the following questions, choose the

... C. a failure to split fructose bisphosphate into triose phosphates. D. a failure to resynthesize glucose from lactic acid. E. excess storage of glycogen. 12. Enzymes affect the rates of chemical reactions by a. displacing the equilibrium constant. b lowering the energy of activation of the reaction. ...
L10v02a_-_glycolysis.stamped_doc
L10v02a_-_glycolysis.stamped_doc

... [00:03:46.71] And then finally pyruvate is the molecule that will be shuttled into the mitochondria for the citric acid cycle. [00:03:53.52] I'd like to look at a detail of step three in glycolysis. As you know, we invested two molecules of ATP. The first ones produces fructose 6-phosphate. At this ...
Lecture 33 Carbohydrates1
Lecture 33 Carbohydrates1

... hydroxyl free radicals. When erythrocytes are exposed to chemicals that generate high levels of superoxide radicals, GSH is required to reduce these damaging compounds. An active pentose phosphate pathway in erythrocytes normally provides sufficient levels of NADPH to maintain the GSH:GSSG ratio at ...
Enzyme Kinetics
Enzyme Kinetics

... • Transition state stabilization is half the story ...
Bioenergetics and ioenergetics and Metabolism etabolism
Bioenergetics and ioenergetics and Metabolism etabolism

... normally be in the form of ATP or a reduced coenzyme (NADH, NADPH). It is noteworthy that the usefulness of ATP as an energy source is not a consequence of any special or ‘high energy’ form of the phosphate bond, but is merely a function of how far the hydrolysis of ATP is displaced from ...
File
File

... The citric acid cycle is the final common pathway for the oxidation of fuel molecules: amino acids, fatty acids, & carbohydrates. • Most fuel molecules enter the cycle as acetyl coenzyme A • This cycle is the central metabolic hub of the cell • It is the gateway to aerobic metabolism for any molecul ...
The Citric Acid Cycle
The Citric Acid Cycle

... The citric acid cycle is the final common pathway for the oxidation of fuel molecules: amino acids, fatty acids, & carbohydrates. • Most fuel molecules enter the cycle as acetyl coenzyme A • This cycle is the central metabolic hub of the cell • It is the gateway to aerobic metabolism for any mol ...
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Nicotinamide adenine dinucleotide



Nicotinamide adenine dinucleotide (NAD) is a coenzyme found in all living cells. The compound is a dinucleotide, because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine base and the other nicotinamide. Nicotinamide adenine dinucleotide exists in two forms, an oxidized and reduced form abbreviated as NAD+ and NADH respectively.In metabolism, nicotinamide adenine dinucleotide is involved in redox reactions, carrying electrons from one reaction to another. The coenzyme is, therefore, found in two forms in cells: NAD+ is an oxidizing agent – it accepts electrons from other molecules and becomes reduced. This reaction forms NADH, which can then be used as a reducing agent to donate electrons. These electron transfer reactions are the main function of NAD. However, it is also used in other cellular processes, the most notable one being a substrate of enzymes that add or remove chemical groups from proteins, in posttranslational modifications. Because of the importance of these functions, the enzymes involved in NAD metabolism are targets for drug discovery.In organisms, NAD can be synthesized from simple building-blocks (de novo) from the amino acids tryptophan or aspartic acid. In an alternative fashion, more complex components of the coenzymes are taken up from food as the vitamin called niacin. Similar compounds are released by reactions that break down the structure of NAD. These preformed components then pass through a salvage pathway that recycles them back into the active form. Some NAD is also converted into nicotinamide adenine dinucleotide phosphate (NADP); the chemistry of this related coenzyme is similar to that of NAD, but it has different roles in metabolism.Although NAD+ is written with a superscript plus sign because of the formal charge on a particular nitrogen atom, at physiological pH for the most part it is actually a singly charged anion (charge of minus 1), while NADH is a doubly charged anion.
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