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Enzymes - Dr. Hamad Ali Yaseen
Enzymes - Dr. Hamad Ali Yaseen

... of another enzyme. This generally arises due to similar but different genes encoding these enzymes and frequently is tissue-type specific or dependent on the growth or developmental status of an organism. ...
Topic guide 1.2: Enzymes
Topic guide 1.2: Enzymes

... pH The optimum pH varies for all enzymes – for many enzymes the optimum pH is pH 7. However, outside their optimum pH range, enzymes are denatured because free hydrogen and hydroxide ions affect the charge of the amino acid. The threedimensional shape is altered, changing the tertiary structure of t ...
Cellular Respiration
Cellular Respiration

... NADH and FADH2 • Donate electrons to the electron transport chain, which powers ATP synthesis via oxidative phosphorylation ...
Fatty Acid Metabolism - University of San Diego Home Pages
Fatty Acid Metabolism - University of San Diego Home Pages

... takes place in the cytosol. A 3 carbon acid malonyl-CoA as the 2 carbon donar. The growing chain is attached to an acyl-carrier protein rather than Co-A. The enzymes are not shared between either Acetyl CoA are produced by pyruvate carboxylase from both glycolytic and TCA intermediates. Acetyl CoA, ...
Dusty Carroll Lesson Plan 4
Dusty Carroll Lesson Plan 4

... formation of dimers, then dimerization of the dimers to form the tetramer. (7) Each domain has a hydrophobic core, consistent with the notion that the monomers formed individually before joining. Some of the domains then interact with each other through polar networks on their exterior surfaces. The ...
lec32_F2015
lec32_F2015

... CoA is a central intermediate  Anabolic role: TCA cycle provides starting material for fats and amino acids. Note: carbohydrates cannot be synthesized from acetyl-CoA by humans. PyruvateAcetyl CoA is one way!  In contrast to glycolysis, none of the intermediates are phosphorylated; but all are ei ...
Ch2
Ch2

... ATP-PCr System • Phosphocreatine (PCr): ATP recycling – PCr + creatine kinase  Cr + Pi + energy – PCr energy cannot be used for cellular work – PCr energy can be used to reassemble ATP ...
Chemistry 20 Chapters 15 Enzymes
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 ...
Biosynthesis of Nucleotides Biosynthesis of Nucleotides
Biosynthesis of Nucleotides Biosynthesis of Nucleotides

... are all contained within a single cytosolic protein. DHO d’hase is localized in the inner mito. membrane. Orotate phosphoribosyltransferase and OMP decarboxylase are contained with a single protein called OMP synthase. ...
Lecture 15 (Parker) - Department of Chemistry ::: CALTECH
Lecture 15 (Parker) - Department of Chemistry ::: CALTECH

... ATP, instead it removes electrons from Acetyl CoA forming NADH and FADH2. These electron carriers yield nine ATP molecules when oxidized by oxidative phosphorylation. Electrons released in the re-oxidation of NADH and FADH2 flow through a series of membrane proteins to generate a proton gradient acr ...
Classification of Enzymes
Classification of Enzymes

... They bind to substrates, but are never covalently attached to substrate or product. They increase the equilibrium constant for a reaction, thus favoring product formation. They increase the stability of the product of a desired reaction by allowing ionizations, resonance, and isomerizations not norm ...
Enzyme
Enzyme

... • It is an organic non-protein group which is tightly bound to the enzyme or as an integral part with the enzyme. • It can act as carriers of atoms or electrons while transferring one compound to another in an overall metabolic pathway. • e.g. FAD, haemoglobin etc. ...
Chapter 15 Review Worksheet and Key
Chapter 15 Review Worksheet and Key

... Calculate the net number of ATPs produced when one 18-carbon fatty acid salt is activated, enters the mitochondrion, and undergoes complete β oxidation. Include the ATP formed from acetyl-CoA in the citric acid cycle, and ATP from all of the reduced coenzymes that are produced. Activation in the fir ...
Enzymes_Group A
Enzymes_Group A

...  For a biochemical reaction to occur, the substrate must closely approach the catalytic site with proper orientation  Once substrate correctly positioned, result in a strained enzyme-substrate complex.  This strain help to bring the enzyme-substrate complex into the transition state  In general, ...
Lipid Metabolism: Power Point presentation
Lipid Metabolism: Power Point presentation

... Reducing agent is NADPH (corresponding oxidation reaction in fatty acid oxidation pathway uses FAD as the oxidizing agent) This cycle repeats using another malonyl–ACP and adding two more carbons. Fatty acid released after seven cycles. ...
Exam 4 key fall 2010
Exam 4 key fall 2010

... Without oxygen electron transport would shut down and NADH and FADH2 could not be reoxidized and all of metabolism would halt. ...
R-C-SCoA (acyl CoA) O
R-C-SCoA (acyl CoA) O

... Such reactions are called displacement reactions because the enzyme displaces a portion of one (or more) of the substrates. The verification of presumed displacement mechanisms such as this one relies upon The Isotope Exchange Technique For a substitution/displacement mechanism of type just describe ...
K m + [S]
K m + [S]

... specifically inhibited. In a process called repression, the end product of a biochemical pathway may inhibit the synthesis of a key enzyme in the pathway. Both induction and repression involve cis-elements, specific DNA sequences located upstream of genes that encode a given enzyme, and a trans-acti ...
Downloadable Full Text - DSpace@MIT
Downloadable Full Text - DSpace@MIT

... of several Fold Type I enzymes that catalyze the transamination of nucleotide sugars in bacteria have been described (19-24). These studies have revealed that while members of this enzyme class share many similarities in the cofactor-binding site, the factors that govern binding and ...
Tricarboxylic Acid Cycle (TCA), Krebs Cycle
Tricarboxylic Acid Cycle (TCA), Krebs Cycle

... pyr dehydrogenase complex is composed of three enzymes – pyr decarboxylase (E1) - dihydrolipoyl transacylase (E2) - dihydrolipoyl dehydrogenase (E3) Each catalyzed a part of the overall reaction In addition to two regulatory enzymes protein kinase and phosphoprotein phosphatase. ...
03-232 Biochemistry         ... Name:________________________ or the back of the preceding page.  In questions... Instructions:
03-232 Biochemistry ... Name:________________________ or the back of the preceding page. In questions... Instructions:

... membrane is 100 mM, and the concentration is 10 mM inside, what is the minimum number of chlorides required to provide enough energy to synthesize one ATP? You can assume that the membrane potential is -100 mV, with the inside negative, and that T=300K. Choice B: The concentration of two short polyp ...
Chapter 5- Enzymes
Chapter 5- Enzymes

... A farm worker accidentally was splashed with a powerful insecticide. A few minutes later, he went into convulsion, stopped breathing, and died. The insecticide was a competitive inhibitor of an enzyme important in the function of the nervous system. 6. Describe the relationship between the structure ...
Lactic Acid fermentation
Lactic Acid fermentation

... Anaerobic Respiration • No oxygen present: ATP can continue to be created through glycolysis – Only 2 ATP produced – Glycolysis stops when all NAD+ is used ...
GLYCOLYSIS - Orange Coast College
GLYCOLYSIS - Orange Coast College

... Importance of phosphorylating glucose ...
Chapter 7 7 The Behavior of Proteins: Enzymes Mechanisms and
Chapter 7 7 The Behavior of Proteins: Enzymes Mechanisms and

... ifi i : catalyzes l the h reaction i off structurally related substrates to give structurally related l d products d • Stereospecificity: catalyzes a reaction in which one stereoisomer is reacted or formed in p preference to all others that might be reacted or formed ...
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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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