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5-2 Necleotide Metabolism (pyrimidine) - Home
5-2 Necleotide Metabolism (pyrimidine) - Home

... phosphate with aspartate with the release of Pi •ATCase is the major site of regulation in bacteria; it is activated by ATP and inhibited by CTP •carbamoyl phosphate is an “activated” compound, so no energy input is needed at this step ...
Enzymes speed up metabolic reactions by lowering energy barriers
Enzymes speed up metabolic reactions by lowering energy barriers

... •  The reactant that an enzyme acts on is called the enzyme’s substrate •  The enzyme binds to its substrate, forming an enzyme-substrate complex •  The active site is the region on the enzyme where the substrate binds •  Induced fit of a substrate brings chemical groups of the active site into posi ...
Recombinant N-terminal Nucleotide
Recombinant N-terminal Nucleotide

... Multidrug resistance of tumor cells is often associated with overexpression of P-glycoprotein, a membrane transporter that extrudes chemotherapeutic drugs using ATP hydrolysis as energy source (1, 2). The protein is encoded by the mdr gene family comprising two members in man, mdr1 and mdr2, or thre ...
design of energy metabolism
design of energy metabolism

... and fats because nitrogenous waste removal incurs a cost. ATP yields are approximately similar to those for carbohydrates. 3. Oxidative Phosphorylation (ETS of IMM) a) NADH or FADH2 from Krebs Cycle are fed through ETS with molecular oxygen serving as the final electron acceptor. ½ O2 reacts with 2 ...
Enzyme - PharmaStreet
Enzyme - PharmaStreet

... • The amino acids serine and cysteine are present in the active sites of some enzymes. These amino acids have nucleophilic residues (OH and SH respectively) which are able to participate in the reaction mechanism. • They do this by reacting with the substrate to form intermediates that would not be ...
CHAPTER 26: Lipid Metabolism - Richest energy source
CHAPTER 26: Lipid Metabolism - Richest energy source

... - we said acetyl CoA formed enters the Krebs cycle, or is used to form Ketone bodies - ketaone bodies are formed from the buildup of acetyl coA in the body with depletion of oxaloacetate = krebs cycle can’t start - caused by diabetes or diet low in carbohydrates (fatty acid oxidation increases to pr ...
CHAPTER 26: Lipid Metabolism
CHAPTER 26: Lipid Metabolism

... ppl must drink a lot of water to accommodate for the extra ketone bodies they are excreting) - Acidosis – ketone bodies are acidic, buildup of acid in blood is acidosis. Interferes with hemoglobin oxygen transport; feeling of lethargy, irritability, loss of apetite - Mammals can convert carbohydrate ...
CO-ENZYMES i.
CO-ENZYMES i.

... catalysts that speed up the pace of chemical reactions. 2. A chemical reaction without an enzyme is like a drive over a mountain. The enzyme bores a tunnel through it so that passage is far quicker and takes much less energy. 3. Enzymes make life on earth possible, all biology from conception to the ...
Ch 16.4 Enzymes and rest
Ch 16.4 Enzymes and rest

... List any facts you know about the molecule shown ...
Amino Acids, Proteins, and Enzymes
Amino Acids, Proteins, and Enzymes

... for the second half of the lab • When your group has agreed on the procedure share it with me for approval • Once it is approved everyone needs to write the procedure into their lab handout • All written procedures, observations, and questions need to be completed in your own words ...
Tutorial: Metabolic Signaling in the b-Cell
Tutorial: Metabolic Signaling in the b-Cell

... triphosphate (ATP), the primary energy molecule. The ATP powers many of the energy-requiring chemical reactions that occur in the cell. However, in b-cells the ATP molecule and several intermediates of metabolism act also as signaling molecules. They tell the b-cell the level of blood glucose, so th ...
Structure, Mechanism, and Disease Implications of Acetyl CoA
Structure, Mechanism, and Disease Implications of Acetyl CoA

... ACC has the typical doubledisplacement kinetics (or ping-pong kinetics) as other biotin-dependent enzymes. It undergoes a two site mechanism in which the binding of a substrate is followed by release of that substrate only to be bound again by the enzymes second domain, then subsequently released as ...
ELECTRON TRANSPORT CHAIN (student)
ELECTRON TRANSPORT CHAIN (student)

... • We need to produce 36 ATP in Cell. Resp. • After 3 stages, we have only produced 6 ATP through substrate-level oxidation • Thus, there are 30 ATP left to create – We produce the remaining 30 ATP through oxidative phosphorylation in the ETC ...
CHAPTER 1 - Portal UniMAP
CHAPTER 1 - Portal UniMAP

... • The binding of one substrate to enzyme facilitates binding of other substrate molecules ...
CHAPTER-IV LIPID METABOLISM BETA
CHAPTER-IV LIPID METABOLISM BETA

... For sources that use the larger ATP production numbers described above, the total would be 129 ATP ={(8-1)*17+12-2} equivalents per palmitate. Beta-oxidation of unsaturated fatty acids changes the ATP yield due to the requirement of two possible additional enzymes. Ketogenesis Ketogenesis is the pro ...
Lecture Notes Ch21
Lecture Notes Ch21

... – A product of a reaction acts as a negative regulator – An end product binds with the first enzyme in a sequence when sufficient product is present ...
Ch 9: E.T.C./ Oxidative Phosphorylation
Ch 9: E.T.C./ Oxidative Phosphorylation

... the mitochondrial membrane, which stores potential energy that can be used to phosphorylate ADP • Some of the proteins in the e.t.c. pump H+ against their gradient…this generates a proton (H+) gradient called the PROTON MOTIVE FORCE. ...
METABOLISM IN HEALTH AND DISEASES I Lecture 2 Pentose
METABOLISM IN HEALTH AND DISEASES I Lecture 2 Pentose

... susceptible to decarboxylation (the second step). • The product of the reaction, riboluso-5-phosphate is the ...
Evolution of Enzymatic Activity in the Enolase Superfamily: Structural
Evolution of Enzymatic Activity in the Enolase Superfamily: Structural

... determined, including the product of the OSBS reaction and three N-acylamino acid substrates for the N-acylamino acid racemase (NAAAR) reaction, N-acetylmethionine, N-succinylmethionine, and Nsuccinylphenylglycine, to 2.2, 2.3, 2.1, and 1.9 Å resolution, respectively. These structures show how the a ...
Photosynthesis
Photosynthesis

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Oxidative degradation of glucose File
Oxidative degradation of glucose File

... 1. GLYCOLYSIS 0R EMBDENMEYERHOFF PATHWAY Glucose is converted into two molecules of pyruvate, chemical energy in the form of ATP is produced, and NADH- reduced coenzymes are produced. This metabolic pathway takes place in almost all cells. All of the enzymes of the glycolysis pathway are found in t ...
Chapter 16 Glycolysis Control of glycolytic pathway
Chapter 16 Glycolysis Control of glycolytic pathway

... The molecule remaining after amylase digestion is limit dextrin, which is rich in α-1, 6-bonds. α-Dextrinase degrades the limit dextran. Sucrase hydrolyzes sucrose, whereas lactase cleaves lactose. ...
Enzymes are Most Effective at Optimal Conditions
Enzymes are Most Effective at Optimal Conditions

... directly proportional to the quantity of enzymes available for it. However, that does not mean that a constant rise in concentration of enzymes will lead to a steady rise in the rate of reaction. Rather, a very high concentration of enzymes where all the substrate molecules are already used up does ...
fates of pyruvate
fates of pyruvate

... FATES OF PYRUVATE -Depends upon presence or absence of O2 - Anaerobic conditions: 1)alcohol fermentation – pyruvate converted to ethyl alcohol 2)lactic acid fermentation - pyruvate converted to lactic acid (cheese, yogurt) - Aerobic conditions: Pyruvate enter the mitochondria where it is completel ...
2nd Phase of Glycolysis
2nd Phase of Glycolysis

... In addition to the allosteric effectors, pyruvate kinase is regulated by covalent modification. Hormones such as glucagon activate a cAMP-dependent protein kinase which transfers the γphosphate of ATP to the pyruvate kinase. The phosphorylated pyruvate kinase is more strongly inhibited by ATP and a ...
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Luciferase



Luciferase is a generic term for the class of oxidative enzymes used in bioluminescence and is distinct from a photoprotein. The name is derived from Lucifer, the root of which means 'light-bearer' (lucem ferre). One example is the firefly luciferase (EC 1.13.12.7) from the firefly Photinus pyralis. ""Firefly luciferase"" as a laboratory reagent often refers to P. pyralis luciferase although recombinant luciferases from several other species of fireflies are also commercially available.
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