cellular respiration jeopardy
... Enzyme that spins as H+ ions pass through and produces ATP A: What is ATP synthase ? S2C06 Jeopardy Review ...
... Enzyme that spins as H+ ions pass through and produces ATP A: What is ATP synthase ? S2C06 Jeopardy Review ...
The Structural Basis of Molecular Adaptation
... Comparing hemoglobins from various species, and using his intimate knowledge of structure–function relations, he chose from a myriad of amino acid replacements those few most likely to be responsible for observed functional differences. In so doing he had attempted to unite form function and phyloge ...
... Comparing hemoglobins from various species, and using his intimate knowledge of structure–function relations, he chose from a myriad of amino acid replacements those few most likely to be responsible for observed functional differences. In so doing he had attempted to unite form function and phyloge ...
Chapter 6
... that uses energy stored in the form of an H+ gradient across a membrane to drive cellular work. – In the mitochondrion, chemiosmosis generates ATP. – Chemiosmosis in chloroplasts also generates ATP, but light drives the electron flow down an electron transport chain and H+ gradient formation. – Prok ...
... that uses energy stored in the form of an H+ gradient across a membrane to drive cellular work. – In the mitochondrion, chemiosmosis generates ATP. – Chemiosmosis in chloroplasts also generates ATP, but light drives the electron flow down an electron transport chain and H+ gradient formation. – Prok ...
Enzymes - Coleg y Cymoedd Moodle
... Rate of reaction depends on how many enzyme molecules there are and the speed they combine with substrate. At first loads and loads of available enzyme molecules for substrate to bind with. So at beginning of reaction often number of enzyme molecules that limits rate. As substrate is converted into ...
... Rate of reaction depends on how many enzyme molecules there are and the speed they combine with substrate. At first loads and loads of available enzyme molecules for substrate to bind with. So at beginning of reaction often number of enzyme molecules that limits rate. As substrate is converted into ...
Chapter 9
... Mechanism Electron transfer in the electron transport chain causes proteins to pump H+ from the mitochondrial matrix to the intermembrane space H+ then moves back across the membrane, passing through the protein complex, ATP synthase ATP synthase uses the exergonic flow of H+ to drive phosphor ...
... Mechanism Electron transfer in the electron transport chain causes proteins to pump H+ from the mitochondrial matrix to the intermembrane space H+ then moves back across the membrane, passing through the protein complex, ATP synthase ATP synthase uses the exergonic flow of H+ to drive phosphor ...
Chapter 15 Enzymes
... • It is synthesized and stored as trypsinogen, which has no enzyme activity. • It becomes active only after a six-amino acid fragment is hydrolyzed and removed from the N-terminal end of its chain. • Removal of this small fragment changes not only the primary structure but also the tertiary structur ...
... • It is synthesized and stored as trypsinogen, which has no enzyme activity. • It becomes active only after a six-amino acid fragment is hydrolyzed and removed from the N-terminal end of its chain. • Removal of this small fragment changes not only the primary structure but also the tertiary structur ...
Unit: Enzymes I
... monitoring is used most commonly with those enzymes in which changes in NADH or NADPH are measured but can also be used for the determination of other enzyme activities (e.g., alkaline phosphatase) if a colored product is generated from a non-colored substrate. Although a few enzyme tests have been ...
... monitoring is used most commonly with those enzymes in which changes in NADH or NADPH are measured but can also be used for the determination of other enzyme activities (e.g., alkaline phosphatase) if a colored product is generated from a non-colored substrate. Although a few enzyme tests have been ...
Chapter 3. Enzymes
... 1) Characteristics of enzyme catalytic reactions: a) enzyme catalytic reactions are thermodynamically possible. Enzymes accelerate reactions by factors of at least a million, but not change the equilibrium; b) enzymes are highly specific for their reactants which are so called “substrates”; ...
... 1) Characteristics of enzyme catalytic reactions: a) enzyme catalytic reactions are thermodynamically possible. Enzymes accelerate reactions by factors of at least a million, but not change the equilibrium; b) enzymes are highly specific for their reactants which are so called “substrates”; ...
幻灯片 1
... They have less potential metabolic energy than the fatty acids from which they are derived but they make up for this deficiency by serving as “water-soluble lipids” that can be more readily transported in the blood plasma. During starvation, ketone bodies are produced in large amounts becoming subst ...
... They have less potential metabolic energy than the fatty acids from which they are derived but they make up for this deficiency by serving as “water-soluble lipids” that can be more readily transported in the blood plasma. During starvation, ketone bodies are produced in large amounts becoming subst ...
Practice Exam III answers
... 11). Some enzymes require a necessary metal ion cofactor for catalysis. Which of the following is not a potential property that a metal ion may impart to an enzymatically catalyzed reaction? a). May act as a super acid. b). May shield and stabilize charges. c). May facilitate redox reactions. d). Ma ...
... 11). Some enzymes require a necessary metal ion cofactor for catalysis. Which of the following is not a potential property that a metal ion may impart to an enzymatically catalyzed reaction? a). May act as a super acid. b). May shield and stabilize charges. c). May facilitate redox reactions. d). Ma ...
Pyruvate - Moodle NTOU
... Mechanism § Electron transfer in the electron transport chain causes proteins to pump H+ from the mitochondrial matrix to the intermembrane space § H+ then moves back across the membrane, passing through the protein complex, ATP synthase § ATP synthase uses the exergonic flow of H+ to drive ph ...
... Mechanism § Electron transfer in the electron transport chain causes proteins to pump H+ from the mitochondrial matrix to the intermembrane space § H+ then moves back across the membrane, passing through the protein complex, ATP synthase § ATP synthase uses the exergonic flow of H+ to drive ph ...
Enzymes - HKEdCity
... living organism. e.g. A + B ↔ C + D 3. An enzyme changes the rate only at which chemical equilibrium is reached; it does not affect the position of the equilibrium. 4. An enzyme speeds up the rate of reaction by lowering the activation energy barrier. 5. It works rapidly and therefore is required in ...
... living organism. e.g. A + B ↔ C + D 3. An enzyme changes the rate only at which chemical equilibrium is reached; it does not affect the position of the equilibrium. 4. An enzyme speeds up the rate of reaction by lowering the activation energy barrier. 5. It works rapidly and therefore is required in ...
23. electron transport and oxidative phosphorylation
... presence of isocitrate dehydrogenase. Conversely, the strongly positive standard potential of H2O/O2 couple, 0.82 V, indicates that water molecule has very little tendency to lose electrons to form molecular oxygen. In other words, molecular oxygen has a very high affinity for electrons or hydrogen ...
... presence of isocitrate dehydrogenase. Conversely, the strongly positive standard potential of H2O/O2 couple, 0.82 V, indicates that water molecule has very little tendency to lose electrons to form molecular oxygen. In other words, molecular oxygen has a very high affinity for electrons or hydrogen ...
Chapter 24 Fatty Acids as Energy Source Fatty Acids as Energy
... phytol in ruminant animals and thus appears in dairy products. ...
... phytol in ruminant animals and thus appears in dairy products. ...
NUCLEOTIDES METABOLISM Nucleotide
... XO in liver, intestines (and milk) can oxidize hypoxanthine (twice) to uric acid Humans and other primates excrete uric acid in the urine, but most N goes out as urea Birds, reptiles and insects excrete uric acid and for them it is the major nitrogen excretory compound Gout occurs from accumulation ...
... XO in liver, intestines (and milk) can oxidize hypoxanthine (twice) to uric acid Humans and other primates excrete uric acid in the urine, but most N goes out as urea Birds, reptiles and insects excrete uric acid and for them it is the major nitrogen excretory compound Gout occurs from accumulation ...
03-232 Biochemistry Exam III - S2014 Name:________________________
... Choice A: Olive oil is a triglyceride that melts at 10oC and is therefore a liquid at room temperature. Coconut oil is a triglyceride that melts at 25oC and is therefore a solid at room temperature. What is the most likely difference between the fatty acids in these two oils and how does this differ ...
... Choice A: Olive oil is a triglyceride that melts at 10oC and is therefore a liquid at room temperature. Coconut oil is a triglyceride that melts at 25oC and is therefore a solid at room temperature. What is the most likely difference between the fatty acids in these two oils and how does this differ ...
The Depth of Chemical Time and the Power of Enzymes
... a few higher values had been recorded at the time of a more recent review.28 Considered together, these findings seemed to suggest that enzymatic and nonenzymatic reactions differ only slightly in their response to changing temperature, implying that the catalytic effect of enzymes is mainly entropi ...
... a few higher values had been recorded at the time of a more recent review.28 Considered together, these findings seemed to suggest that enzymatic and nonenzymatic reactions differ only slightly in their response to changing temperature, implying that the catalytic effect of enzymes is mainly entropi ...
The Depth of Chemical Time and the Power of Enzymes as Catalysts
... a few higher values had been recorded at the time of a more recent review.28 Considered together, these findings seemed to suggest that enzymatic and nonenzymatic reactions differ only slightly in their response to changing temperature, implying that the catalytic effect of enzymes is mainly entropi ...
... a few higher values had been recorded at the time of a more recent review.28 Considered together, these findings seemed to suggest that enzymatic and nonenzymatic reactions differ only slightly in their response to changing temperature, implying that the catalytic effect of enzymes is mainly entropi ...
Fundamentals: Bioenergetics and Enzyme Function
... 5. Why is the D and I structure interpretation of glycogen synthetase activity no longer acceptable? 6. Understand and apply the terminology of the A0.5 for G6P and the S0.5 for UDPglucose to the in vivo regulation of synthetase? 7. Do the enzyme activation curves for synthetase indicate Michaelis M ...
... 5. Why is the D and I structure interpretation of glycogen synthetase activity no longer acceptable? 6. Understand and apply the terminology of the A0.5 for G6P and the S0.5 for UDPglucose to the in vivo regulation of synthetase? 7. Do the enzyme activation curves for synthetase indicate Michaelis M ...
Chemistry 20 Chapters 15 Enzymes
... Noncompetitive inhibitor: the structure of a noncompetitive inhibitor does not resemble the substrate and does not compete for the active site. Instead, a noncompetitive inhibitor binds to a site on the enzyme that is not the active site. When the noncompetitive inhibitor is bonded to the enzyme, th ...
... Noncompetitive inhibitor: the structure of a noncompetitive inhibitor does not resemble the substrate and does not compete for the active site. Instead, a noncompetitive inhibitor binds to a site on the enzyme that is not the active site. When the noncompetitive inhibitor is bonded to the enzyme, th ...
Ch. 6 Cell Respiration.notebook
... When there is oxidation, there is also reduction. The substance which loses electrons is oxidised. The substance which gains electrons is reduced. ...
... When there is oxidation, there is also reduction. The substance which loses electrons is oxidised. The substance which gains electrons is reduced. ...
Bioinformatik - Chair of Computational Biology
... grouped into `traditional pathways' (e.g. glycolysis) that do not account for cofactors and byproducts in a way that lends itself to a mathematical description. However, with sequenced and annotated genomes, models can be made that account for many metabolic reactions in ...
... grouped into `traditional pathways' (e.g. glycolysis) that do not account for cofactors and byproducts in a way that lends itself to a mathematical description. However, with sequenced and annotated genomes, models can be made that account for many metabolic reactions in ...
Shedding Light on the Bioluminescence “Paradox”
... stered this argument with evidence that reconnection between the lux system and resisductant flows through luciferase only when tance to oxidative stress, although an alderespiration is saturated. They speculate that luhyde-deficient dark mutant is also resistant. minescence becomes important for sy ...
... stered this argument with evidence that reconnection between the lux system and resisductant flows through luciferase only when tance to oxidative stress, although an alderespiration is saturated. They speculate that luhyde-deficient dark mutant is also resistant. minescence becomes important for sy ...
Metabolism
... • Glycolysis generates 2 ATP and 2 NADH • Two ATP are used in energy-investment to add phosphate groups to glucose and fructose-6-phosphate • Four ATP are formed in energy-generation by direct transfers of phosphate groups to four ADP. Glucose + 2ADP + 2Pi + 2NAD+ 2Pyruvate + 2ATP + 2NADH + 4H+ ...
... • Glycolysis generates 2 ATP and 2 NADH • Two ATP are used in energy-investment to add phosphate groups to glucose and fructose-6-phosphate • Four ATP are formed in energy-generation by direct transfers of phosphate groups to four ADP. Glucose + 2ADP + 2Pi + 2NAD+ 2Pyruvate + 2ATP + 2NADH + 4H+ ...
16. enzymes i – nomenclature and classification
... Sumner and Myrbäck (1950) have beautifully defined the enzymes as ‘simple or combined proteins acting as specific catalysts’. They are soluble, colloidal molecules which are produced by living cells. All enzymes are globular proteins with a complex 3-‘D’ structure, capable of binding substrate molec ...
... Sumner and Myrbäck (1950) have beautifully defined the enzymes as ‘simple or combined proteins acting as specific catalysts’. They are soluble, colloidal molecules which are produced by living cells. All enzymes are globular proteins with a complex 3-‘D’ structure, capable of binding substrate molec ...
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.