Structural Biochemistry/Enzyme
... assigned names by the type of reaction they catalyze. This allowed for the addition of a four-digit number that would precede EC(Enzyme Commission) and each enzyme could be identified. The reaction that an enzyme catalyzes must be know before it can be classified. Oxidoreductases catalyze oxidation- ...
... assigned names by the type of reaction they catalyze. This allowed for the addition of a four-digit number that would precede EC(Enzyme Commission) and each enzyme could be identified. The reaction that an enzyme catalyzes must be know before it can be classified. Oxidoreductases catalyze oxidation- ...
AnSc 5311 Ruminant Nutrition Microbial Fermentation of
... ATP yield seems to be 1 mole per 3 moles of lactate because the acyldehydrogenase does not seem to be linked to phosphorylation ...
... ATP yield seems to be 1 mole per 3 moles of lactate because the acyldehydrogenase does not seem to be linked to phosphorylation ...
16-18 Cellular respiration
... A German-British scientist, Hans Krebs, elucidated this catabolic pathway in the 1930s. The Krebs cycle, which is also known as the citric acid cycle, has eight enzyme-controlled steps that occur in the mitochondrial matrix. ...
... A German-British scientist, Hans Krebs, elucidated this catabolic pathway in the 1930s. The Krebs cycle, which is also known as the citric acid cycle, has eight enzyme-controlled steps that occur in the mitochondrial matrix. ...
Regeneration of Cofactors for Enzyme Biocatalysis
... reflects several important factors such as concentration and degradation of the cofactor over time, regioselectivity of regeneration, rate of catalysis, and time of reaction. Additionally, the availability of regenerative enzymes or reagents and their stability under process conditions is an importa ...
... reflects several important factors such as concentration and degradation of the cofactor over time, regioselectivity of regeneration, rate of catalysis, and time of reaction. Additionally, the availability of regenerative enzymes or reagents and their stability under process conditions is an importa ...
Mechanism of enzyme action, kinetic of enzymatic catalysis
... •Inhibitor binds as a substrate and is initially processed by the normal catalytic mechanism •It then generates a chemically reactive intermediate that inactivates the enzyme through covalent modification •Suicide because enzyme participates in its own irreversible inhibition ...
... •Inhibitor binds as a substrate and is initially processed by the normal catalytic mechanism •It then generates a chemically reactive intermediate that inactivates the enzyme through covalent modification •Suicide because enzyme participates in its own irreversible inhibition ...
Cellular Respiration 2016
... • During lactic acid fermentation, pyruvate is reduced directly by NADH to form lactate (ionized form of lactic acid). • Lactic acid fermentation by some fungi and bacteria is used to make cheese and yogurt. • Muscle cells switch from aerobic respiration to lactic acid fermentation to generate ATP ...
... • During lactic acid fermentation, pyruvate is reduced directly by NADH to form lactate (ionized form of lactic acid). • Lactic acid fermentation by some fungi and bacteria is used to make cheese and yogurt. • Muscle cells switch from aerobic respiration to lactic acid fermentation to generate ATP ...
Cellular Respiration Breathe in… breathe out… or not!
... • During lactic acid fermentation, pyruvate is reduced directly by NADH to form lactate (ionized form of lactic acid). • Lactic acid fermentation by some fungi and bacteria is used to make cheese and yogurt. • Muscle cells switch from aerobic respiration to lactic acid fermentation to generate ATP ...
... • During lactic acid fermentation, pyruvate is reduced directly by NADH to form lactate (ionized form of lactic acid). • Lactic acid fermentation by some fungi and bacteria is used to make cheese and yogurt. • Muscle cells switch from aerobic respiration to lactic acid fermentation to generate ATP ...
Label-free and redox proteomic analyses of the
... intracellular lipids in Rhodococcus strains were performed by TLC. For intracellular analysis, 4–5 mg of lyophilized cells were extracted with a mixture of chloroform and methanol (2 : 1, v/v) for 120 min at 4 uC. Fifteen to thirty microlitres of extracts (depending on culture conditions) were separ ...
... intracellular lipids in Rhodococcus strains were performed by TLC. For intracellular analysis, 4–5 mg of lyophilized cells were extracted with a mixture of chloroform and methanol (2 : 1, v/v) for 120 min at 4 uC. Fifteen to thirty microlitres of extracts (depending on culture conditions) were separ ...
Biomolecules
... Proteolysis, amino acid pool, metabolic flow of amino acid nitrogen, fate of carbon skeletons, biosynthesis of other amino acid-derived compounds, heme metabolism. Nucleotide metabolism Synthesis of purine and pymiridine nucleotides Degradation of purines and pyrimidines, inhibition of purine and py ...
... Proteolysis, amino acid pool, metabolic flow of amino acid nitrogen, fate of carbon skeletons, biosynthesis of other amino acid-derived compounds, heme metabolism. Nucleotide metabolism Synthesis of purine and pymiridine nucleotides Degradation of purines and pyrimidines, inhibition of purine and py ...
Chem*3560 Lecture 6: Allosteric regulation of enzymes
... When ATP and CTP are both present, they compete for the same binding site (see below), and the relative concentration of the two nucleotides will determine whether a positive or negative effect is observed. CTP has slightly more affinity, so [ATP] has to be significantly higher than [CTP] for a posi ...
... When ATP and CTP are both present, they compete for the same binding site (see below), and the relative concentration of the two nucleotides will determine whether a positive or negative effect is observed. CTP has slightly more affinity, so [ATP] has to be significantly higher than [CTP] for a posi ...
09_Lectures_PPT
... • 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 channels in ATP synthase • ATP synthase uses the exergonic flow of H+ to drive phosphorylation of ATP ...
... • 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 channels in ATP synthase • ATP synthase uses the exergonic flow of H+ to drive phosphorylation of ATP ...
LACTATE/PYRUVATE RATIO Relevant disorders Related
... Pyruvate should only be analysed when lactate is elevated to determine the patients redox state. Pyruvate is an end product of glycolysis. It can either be converted to lactate under anaerobic conditions or transported into mitochondria to feed into the Kreb’s cycle under aerobic conditions. Lactate ...
... Pyruvate should only be analysed when lactate is elevated to determine the patients redox state. Pyruvate is an end product of glycolysis. It can either be converted to lactate under anaerobic conditions or transported into mitochondria to feed into the Kreb’s cycle under aerobic conditions. Lactate ...
Gluconeogenesis by Dr Tarek
... non-carbohydrate precursors • In other words: – Create new glucose from the products of its breakdown ...
... non-carbohydrate precursors • In other words: – Create new glucose from the products of its breakdown ...
Enzymes: The Biological Catalysts of Life
... and conversion of chemical energy. Enzyme catalysis is essential for making biochemical reactions proceed at appropriate speed in physiological conditions. They speed up the reactions in the cells so that they may occur in fractions of seconds. In the absence of catalysts most cellular reactions wou ...
... and conversion of chemical energy. Enzyme catalysis is essential for making biochemical reactions proceed at appropriate speed in physiological conditions. They speed up the reactions in the cells so that they may occur in fractions of seconds. In the absence of catalysts most cellular reactions wou ...
CHAPTER 4: Enzyme Structure
... The substrate molecule is complementary in shape to that of the active site. It was thought that the substrate exactly fitted into the active site of the enzyme molecule like a key fitting into a lock (the now discredited ‘lock and key’ theory). This explained why an enzyme would only work on one su ...
... The substrate molecule is complementary in shape to that of the active site. It was thought that the substrate exactly fitted into the active site of the enzyme molecule like a key fitting into a lock (the now discredited ‘lock and key’ theory). This explained why an enzyme would only work on one su ...
October 15 AP Biology - John D. O`Bryant School of Math & Science
... blocks enzyme bacteria use to build cell walls disulfiram (Antabuse) treats chronic alcoholism blocks enzyme that ...
... blocks enzyme bacteria use to build cell walls disulfiram (Antabuse) treats chronic alcoholism blocks enzyme that ...
C - 鄭智美的Homepage
... chemiosmosis couples electron transport to ATP synthesis NADH and FADH2 – Donate electrons to the electron transport chain, which powers ATP synthesis via oxidative phosphorylation ...
... chemiosmosis couples electron transport to ATP synthesis NADH and FADH2 – Donate electrons to the electron transport chain, which powers ATP synthesis via oxidative phosphorylation ...
enzymes - Yengage
... Catalytic sites of enzymes contain sites for binding cofactors or coenzymes exists d/t tertiary structure of protein loss of native enzyme structure derangement of active site loss of function ...
... Catalytic sites of enzymes contain sites for binding cofactors or coenzymes exists d/t tertiary structure of protein loss of native enzyme structure derangement of active site loss of function ...
Finals Practice Exam answers
... homogenate, paying specific attention to separating Pyruvate Dehydrogenase from -ketoglutarate Dehydrogenase, Aconitase from Malate Dehydrogenase, and Succinyl-CoA Thiokinase from Fumarase in their native states, using affinity chromatography only as a last resort. : Size exclusion chromatography ...
... homogenate, paying specific attention to separating Pyruvate Dehydrogenase from -ketoglutarate Dehydrogenase, Aconitase from Malate Dehydrogenase, and Succinyl-CoA Thiokinase from Fumarase in their native states, using affinity chromatography only as a last resort. : Size exclusion chromatography ...
Lecture 30
... History Present Illness: Baby was treated for anemia by family doctor but did not respond to vitamin B12, folic acid, iron or vitamin C. She is the third-born child of a healthy white couple; her mother had an uneventful pregnancy and a eutopic delivery. Both brothers are healthy. Physical Exam: Low ...
... History Present Illness: Baby was treated for anemia by family doctor but did not respond to vitamin B12, folic acid, iron or vitamin C. She is the third-born child of a healthy white couple; her mother had an uneventful pregnancy and a eutopic delivery. Both brothers are healthy. Physical Exam: Low ...
Gluconeogenesis
... starvation is mainly amino acid catabolism. Some amino acids are catabolized to pyruvate, oxaloacetate, or precursors of these. Muscle proteins may break down to supply amino acids. These are transported to liver where they are deaminated and converted to gluconeogenesis inputs. Glycerol, derived fr ...
... starvation is mainly amino acid catabolism. Some amino acids are catabolized to pyruvate, oxaloacetate, or precursors of these. Muscle proteins may break down to supply amino acids. These are transported to liver where they are deaminated and converted to gluconeogenesis inputs. Glycerol, derived fr ...
Cellular Respiration: Harvesting Chemical Energy
... In the third stage of respiration, the electron transport chain accepts electrons from the breakdown products of the first two stages (most often via NADH). In the electron transport chain, the electrons move from molecule to molecule until they combine with molecular oxygen and hydrogen ions to for ...
... In the third stage of respiration, the electron transport chain accepts electrons from the breakdown products of the first two stages (most often via NADH). In the electron transport chain, the electrons move from molecule to molecule until they combine with molecular oxygen and hydrogen ions to for ...
Chapter 9
... The Pathway of Electron Transport • Electrons are transferred from NADH or FADH2 to the electron transport chain • Electrons are passed through a number of proteins including cytochromes (each with an iron atom) to O2 • The electron transport chain generates no ATP • The chain’s function is to brea ...
... The Pathway of Electron Transport • Electrons are transferred from NADH or FADH2 to the electron transport chain • Electrons are passed through a number of proteins including cytochromes (each with an iron atom) to O2 • The electron transport chain generates no ATP • The chain’s function is to brea ...
A-level Human Biology Question paper Unit 5 - Inheritance
... oxidation of reduced NAD and reduced FAD. Palmitic acid was respired aerobically in the presence of DNP. This resulted in a net yield of only 6 molecules of ATP per molecule of palmitic acid. Use information from Figure 1 and from Equation 2 to suggest why. ...
... oxidation of reduced NAD and reduced FAD. Palmitic acid was respired aerobically in the presence of DNP. This resulted in a net yield of only 6 molecules of ATP per molecule of palmitic acid. Use information from Figure 1 and from Equation 2 to suggest why. ...
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.