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2.-lactic-acid-metabolism
2.-lactic-acid-metabolism

... Oxygen debt builds up Oxygen debt ...
Document
Document

... oxidation of carbs, protein and fatty acids, are ultimately transferred to O2 to produce H20  Located in the inner mitochondrial membrane  Electrons travel down the chain, pumping protons into the intermembrane space creating the driving force to produce ATP in a process called oxidative phosphory ...
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PowerPoint 簡報

... • Fermentation is referring to the process when no oxygen is consumed or no change in the concentration of NAD+ or NADH during energy extraction. ...
The Citric acid cycle
The Citric acid cycle

... It is called the Krebs cycle or the tricarboxylic and is the “hub” of the metabolic system. It accounts for the majority of carbohydrate, fatty acid and amino acid oxidation. It also accounts for a majority of the generation of these compounds and others as well. Amphibolic - acts both catabolically ...
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... Metabolism—the sum of all biochemical reactions in an organism or cell. a) anabolic—synthesis of compounds; an example is photosynthesis b) catabolic—breakdown of compounds; an example is cellular respiration Metabolic pathways—are the steps (enzymes, substrates and products) used or followed to con ...
2nd Phase of Glycolysis
2nd Phase of Glycolysis

... NADH produced from one molecule of glucose during glycolysis have three possible metabolic fates. Under aerobic conditions, pyruvate is oxidized, with the loss of CO2 to produce acetyl-CoA and NADH. AcetylCoA then enters the citric acid cycle where it is completely oxidized into CO2 and H2O. Under a ...
2. Glucogenic amino acids
2. Glucogenic amino acids

... the major role in maintaining the blood glucose level. 2. During starvation, Gluconeogenesis maintains normal blood glucose level. The stored glycogen is depleted within the first 12-18 hours of fasting. On prolonged starvation, the gluconeogenesis is speeded up and protein catabolism provides the s ...
Chapter 9 - Angelfire
Chapter 9 - Angelfire

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PYRUVATE DEHYDROGENASE COMPLEX
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emboj7601444-sup

... between the two moieties, was expressed in E. coli BL-21 (DE3) cells, similar to the method described previously (Wynn et al., 1994). Mutations were introduced using the QuickChange site-directed mutagenesis system from Stratagene (La Jolla, CA). The fusion proteins were purified with amylose resin, ...
Lactate - University of Iowa Health Care
Lactate - University of Iowa Health Care

... Second, the maximal glycolytic capacity of muscle exceeds the maximal oxidative capacity. In glycolysis, the NAD+ pool is consumed as electron acceptor and it must be recycled. Recycling of NAD+ is done by converting pyruvate and NADH to lactate and NAD+ during extreme muscular activity. This reacti ...
Nuclear Chemistry
Nuclear Chemistry

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Glycolysis - medscistudents
Glycolysis - medscistudents

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GLUCONEOGENESIS
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... The source of pyruvate and oxaloacetate for gluconeogenesis during fasting or carbohydrate 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 l ...
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... • Muscles lack pyruvate dehydrogenase and cannot produce ethanol from pyruvate • Muscle lactate dehydrogenase converts pyruvate to lactate • This reaction regenerates NAD+ for use by glyceraldehyde 3phosphate dehydrogenase in glycolysis • Lactate formed in skeletal muscles during exercise is transpo ...
Table S1. - BioMed Central
Table S1. - BioMed Central

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Ch18.doc
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... by pyruvate dehydrogenase (1 NADH) and one turn of the CAC: yielding 3NADH, 1FADH2 and 1 GTP. Converting NADH and FADH2 to ATPs we use 1 NADH = 2.5 ATP and 1 FADH2 = 1.5 ATP. So for one lactate: (3+1+1)(2.5 ATP) + 1.5 ATP + 1 ATP = 15 ATP. From alanine, it is the transaminase reaction, then pyruvate ...
Valine Mydrogenase from Streptmzyces fiadipe
Valine Mydrogenase from Streptmzyces fiadipe

... Valine dehydrogenase (VDH ; EC 1.4.1.8) activity was detected in a cell-free extract of Streptomycesfiadk in which it was thought to be a mgulatory enzyme involved in biosynthesis of n-butyrate, a buiiding unit of the oligoketideantibiotictylosin ( b u r a et al., 1983). Inhibition of VDH synthesisa ...
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... In the last few years our interest has been devoted to the energy metabolism of the eggs of the common toad Bufo arenarum Hensel which, like some other amphibian eggs, can cleave at a normal rate in the absence of oxygen or in the presence of cyanide (Barbieri & Legname, 1957). Under anaerobic condi ...
Zhang Yufeng - USD Biology
Zhang Yufeng - USD Biology

... • CBF and CMRglc increase more than oxygen utilization, and • Both oxidative and nonoxidative processes are involved to meet the increased metabolic ...
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Exam 3

... Bonus: (5 pts) How many protons are transferred into the intermembrane space of a mitochondria when one molecule of lactate is fully processed through the citric acid cycle? Give a full and clear accounting of your thought process to receive any credit. (Assume that any cytosolic NADH produced go t ...
GLYCOLYSIS AND GLUCONEOGENESIS
GLYCOLYSIS AND GLUCONEOGENESIS

... effect on glycolysis. This makes a great exam question. Arsenate is a substrate for the enzyme glyceraldehyde-3-phosphate dehydrogenase. The enzyme, which normally uses phosphate and makes 1,3-disphosphoglycerate, is fooled by the arsenate and makes the arsenate ester instead. With the phosphate est ...
213 lactate dehydrog..
213 lactate dehydrog..

... absence of mitochondria and muscle during exercises due to oxygen lack. ...
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Lactate dehydrogenase



A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another.LDH exist in four distinct enzyme classes. This article is about the common NAD(P)-dependent L-lactate dehydrogenase. Other LDHs act on D-lactate and/or are dependent on cytochrome c: D-lactate dehydrogenase (cytochrome)) and L-lactate (L-lactate dehydrogenase (cytochrome)). LDH has been of medical significance because it is found extensively in body tissues, such as blood cells and heart muscle. Because it is released during tissue damage, it is a marker of common injuries and disease such as heart failure.
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