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... Therefore enzymes are catalysts because they speed up biochemical reactions • We need enzymes for every process that happens in our bodies! e.g. Digesting food, replicating DNA ...
Glycolysi
Glycolysi

... Irreversible, committed step in glycolysis Activation under low [ATP] or high [ADP and AMP] Phosphoryl group donor  ATP  PPi : some bacteria and protist, all plants ...
Amino acid sequence alignment of a `small` citrate synthase from
Amino acid sequence alignment of a `small` citrate synthase from

... cerevisiae is well documented [3], evidence has now been provided suggesting the presence of two CS genes in Escherichia coli [4] and Bacillus subtilis [S], organisms considered for many years to contain a single molecular form of CS. There is also evidence that CS isoenzymes may have different meta ...
Fundamentals of Biochemistry
Fundamentals of Biochemistry

... in order to regenerate NAD+ (from NADH)—which is required for the continuity of anaerobic glycolysis—in a process known as “homolactic fermentation” ...
CONTRIBUTIONS OF ANAEROBIC METABOLISM TO pH
CONTRIBUTIONS OF ANAEROBIC METABOLISM TO pH

... reactions involved in energy production during catabolism of fats, carbohydrates, proteins or amino acids. Oxidation involves the transformation of saturated into unsaturated substances, the formation of carbonyl groups from alcohols, and finally yields acidic carboxyl groups. During formation, howe ...
PPT
PPT

... – The molecules of electron transport chains are built into the inner membranes of mitochondria. • The chain functions as a chemical machine that uses energy released by the “fall” of electrons to pump hydrogen ions across the inner mitochondrial ...
2015
2015

... β-lactamase; bacteria chymotrypsin; bacteria lysozyme; human cells transpeptidase; bacteria aldolase; bacteria ...
- Circle of Docs
- Circle of Docs

... a. ascorbic acid b. cholecalciferol c. retinal d. tocopherol 38. responsible for the transportation of iron in the blood a. ferritin b. ferrous sulfate c. ferric sulfate d. transferrin 39. hemoglobin contains a. 4 alpha globulin chains b. 4 binding sites to oxygen c. 4 beta globulin chains d. iron ...
Cellular respiration
Cellular respiration

... enter the mitochondrion and are completely broken down, yielding two ATP and ten high-energy electron carriers: eight NADH and two FADH2. The carbon atoms from the pyruvates are released in six molecules of CO2 – High-energy electrons release energy that is harnessed to pump H into the intermembran ...
Enzymes are macromolecules that help accelerate (catalyze
Enzymes are macromolecules that help accelerate (catalyze

... Transferases catalyze group transfer reactions. The transfer occurs from one molecule that will be the donor to another molecule that will be the acceptor. Most of the time, the donor is a cofactor that is charged with the group about to be transferred. Hydrolases catalyze reactions that involve hyd ...
Property it tests for
Property it tests for

...  Use FRESH reagent, less than a couple of hours old (it is taken out of the freezer).  Pick your inoculum, not with a metal loop (reagent may react with the metal), but with a wooden stick.  Read the reaction within 20 seconds (NOT after), usually it will change in less than 15 seconds. The oxyge ...
10.25-11.3.11 Glycolysis
10.25-11.3.11 Glycolysis

... •Cells are far away from equilibrium and far away from standard state conditions. We have much more ATP than would be dictated by equilibrium; the ratio of ATP to ADP+Pi in some cells is as high as 200/1 rather than 1/200,000. •This means that a cell can be far from equilibrium w.r. to this ratio, a ...
acid
acid

... using NADH as hydrogen donor is essential for the continuation of glycolysis in rapidly contracting skeletal muscle and erythrocytes because NADH can not be oxidized by respiratory chain O2 been reduced to NADH. By reducing pyruvate to lactate and oxidizing NADH to NAD, lactate dehydrogenase prevent ...


... Protein phosphorylation is used to coordinately regulate glycogen synthesis and degradation. Glycogen phosphorylase is active when phosphorylated since the phosphorylation state of proteins is high when glucose levels are low. (2 pts for statements along these lines). Therefore glycogen synthase sho ...
enzyme
enzyme

... Competitive Inhibition: The inhibitor competes with the substrate or coenzyme for the binding site on the active center by forming an enzyme inhibitor complex EI. Inhibition can be made ineffective by excess substrate, as is the case for inhibition of succinate dehydrogenase by malonate. ...
Glossary of Key Terms in Chapter Two
Glossary of Key Terms in Chapter Two

... absolute specificity (19.5) the property of certain enzymes that allows them to bind and catalyze the reaction of only one substrate. active site (19.4) the cleft in the surface of an enzyme that is the site of substrate binding. allosteric enzymes (19.9) enzymes that have an effector binding site a ...
Full research publication
Full research publication

... proton signals mono methine proton at δ 5,67 ppm, mono amino proton NH-chelate at δ 14,70 ppm mono and two methylene protons of the methyl acetate moiety at δ 3,67 ppm integral with comparable intensities are present. Furthermore predominant form of monohelatnoy 2B is present in the spectrum signals ...
Block 1 Unit #3
Block 1 Unit #3

... b. Glucokinase in liver (duringgluckose state) 7. Name the regulatory enzymes in glycolysis a. Hexokinase, Phosphofructokinase, pyruvate kinase 8. What role does dihydroxyacetone phosphate play in a) glycolysis b) triglyceride synthesis c) in the glycerol phosphate shuttle? a. Glycolysis – dihydrox ...
Ex Phys 2 Wiki
Ex Phys 2 Wiki

... VCO2: volume of CO2 produced **at SUBMAX the trained individual will use less O2. At MAX the trained individual has increased VO2 max so they use more O2 Lactate threshold = anaerobic threshold This is the point at which production > clearance EPOC: excess post-exercise oxygen consumption Not necess ...
The b-oxidation pathway as an energy source
The b-oxidation pathway as an energy source

... 3. 11 residues from number 70 - 80 lining a hydrophobic crevice have remained virtually unchanged throughout all cytochrome c regardless of species or even kingdom. 4. A number of invariant arginine and lysine clusters can be found on the surface of the molecule. Cytochrome c has a dual function in ...
9–1 Chemical Pathways - Springboro Community Schools
9–1 Chemical Pathways - Springboro Community Schools

... How much energy is actually present in food? Quite a lot, although it varies with the type of food, since our cells can use all sorts of molecules as food, including fats, sugars, and proteins. One gram of the sugar glucose (C6H12O6), when burned in the presence of oxygen, releases 3811 calories of ...
Protein Digestion by Enzymes
Protein Digestion by Enzymes

... Protein Digestion by Enzymes Introduction: Almost every chemical reaction in the body is catalyzed by a class of proteins called enzymes. There are two main types of enzymes, metabolic and digestive enzymes. The unique amino acid sequence and shape of an enzyme determines its function. Digestive enz ...
CHAPTER 6
CHAPTER 6

... When the ADP/ATP or NAD+/NADH ratio is high, the TCA cycle is turned on Succinyl-CoA is an intracycle regulator, inhibiting citrate synthase and ketoglutarate dehydrogenase Acetyl-CoA acts as a signal to the TCA cycle that glycolysis and fatty acid breakdown is producing two-carbon unit ...
O usually has oxidation number of -2, except in peroxides where it is
O usually has oxidation number of -2, except in peroxides where it is

... The sum of the oxidation numbers of the elements in a polyatomic ion must equal the ion charge. Consider these examples. If there are two poly atomic ions in a compound deal with them first. ...
Lecture 3: Protein trafficking between cell compartments The cytosol
Lecture 3: Protein trafficking between cell compartments The cytosol

... either lysosomes or cell surface is carried out by transport vesicles (liposomes made of phospholipids) ...
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Oxidative phosphorylation



Oxidative phosphorylation (or OXPHOS in short) is the metabolic pathway in which the mitochondria in cells use their structure, enzymes, and energy released by the oxidation of nutrients to reform ATP. Although the many forms of life on earth use a range of different nutrients, ATP is the molecule that supplies energy to metabolism. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is probably so pervasive because it is a highly efficient way of releasing energy, compared to alternative fermentation processes such as anaerobic glycolysis.During oxidative phosphorylation, electrons are transferred from electron donors to electron acceptors such as oxygen, in redox reactions. These redox reactions release energy, which is used to form ATP. In eukaryotes, these redox reactions are carried out by a series of protein complexes within the inner membrane of the cell's mitochondria, whereas, in prokaryotes, these proteins are located in the cells' intermembrane space. These linked sets of proteins are called electron transport chains. In eukaryotes, five main protein complexes are involved, whereas in prokaryotes many different enzymes are present, using a variety of electron donors and acceptors.The energy released by electrons flowing through this electron transport chain is used to transport protons across the inner mitochondrial membrane, in a process called electron transport. This generates potential energy in the form of a pH gradient and an electrical potential across this membrane. This store of energy is tapped by allowing protons to flow back across the membrane and down this gradient, through a large enzyme called ATP synthase; this process is known as chemiosmosis. This enzyme uses this energy to generate ATP from adenosine diphosphate (ADP), in a phosphorylation reaction. This reaction is driven by the proton flow, which forces the rotation of a part of the enzyme; the ATP synthase is a rotary mechanical motor.Although oxidative phosphorylation is a vital part of metabolism, it produces reactive oxygen species such as superoxide and hydrogen peroxide, which lead to propagation of free radicals, damaging cells and contributing to disease and, possibly, aging (senescence). The enzymes carrying out this metabolic pathway are also the target of many drugs and poisons that inhibit their activities.
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