Lecture 4, Exam III Worksheet Answers
... Thymine dimers within DNA. Two thymines beside each other are bonded together by a covalent bond. Nuclease. It is an enzyme that cleaves nucleic acids. Other enzymes that may be needed in this process are the enzymes needed to create DNA and link it together: primase, both DNA polymerases, and ligas ...
... Thymine dimers within DNA. Two thymines beside each other are bonded together by a covalent bond. Nuclease. It is an enzyme that cleaves nucleic acids. Other enzymes that may be needed in this process are the enzymes needed to create DNA and link it together: primase, both DNA polymerases, and ligas ...
Macromolecules
... structure is distorted or destroyed by heat / ionic concentration / pH change, then the protein is said to be ‘denatured’. Denatured proteins cannot function any more. Enzymes speed up the rates of Chemical Reactions ● They speed up the rate of chemical reactions by increasing the change of molecula ...
... structure is distorted or destroyed by heat / ionic concentration / pH change, then the protein is said to be ‘denatured’. Denatured proteins cannot function any more. Enzymes speed up the rates of Chemical Reactions ● They speed up the rate of chemical reactions by increasing the change of molecula ...
Enzyme
... control metabolism • A cell’s metabolic pathways --- Must be tightly regulated --- by controlling when and where its various enzymes are active. * The molecular that naturally regulate enzyme activity in a cell behave like reversible noncompetitive inhibitors. * Allosteric regulation --- Is the term ...
... control metabolism • A cell’s metabolic pathways --- Must be tightly regulated --- by controlling when and where its various enzymes are active. * The molecular that naturally regulate enzyme activity in a cell behave like reversible noncompetitive inhibitors. * Allosteric regulation --- Is the term ...
Keshara Senanayake Ms.Reep AP BIOLOGY Chapter 6
... real life 78% greater energy is released by ATP hydrolysis under STC) >since hydrolysis release energy because note that the reactants (ATP and water) are high energy RELATIVE to the energy of the products (ADP and (P)i) release of energy during hydrolysis of ATP comes from the chemical change to ...
... real life 78% greater energy is released by ATP hydrolysis under STC) >since hydrolysis release energy because note that the reactants (ATP and water) are high energy RELATIVE to the energy of the products (ADP and (P)i) release of energy during hydrolysis of ATP comes from the chemical change to ...
Chapter 8 Summary
... and the breakdown of energy-yielding nutrients. Chemical reactions are catalyzed by enzymes, some requiring cofactors or coenzymes to function. A cofactor is an inorganic substance that is part of the enzyme’s structure. Coenzymes are organic molecules that assist enzymes in redox reactions by trans ...
... and the breakdown of energy-yielding nutrients. Chemical reactions are catalyzed by enzymes, some requiring cofactors or coenzymes to function. A cofactor is an inorganic substance that is part of the enzyme’s structure. Coenzymes are organic molecules that assist enzymes in redox reactions by trans ...
Anatomy & Physiology
... Hormones-chemical messengers carried in the blood that stimulate target cells. Transport proteins-carry materials in the blood (hemoglobin) and across cell membranes Catalysts (Enzymes)-act as biological catalysts, to regulate and accelerate the rate of biochemical reactions without being used up in ...
... Hormones-chemical messengers carried in the blood that stimulate target cells. Transport proteins-carry materials in the blood (hemoglobin) and across cell membranes Catalysts (Enzymes)-act as biological catalysts, to regulate and accelerate the rate of biochemical reactions without being used up in ...
classsssssss
... male who suffers from periodic hemolysis demonstrate a low activity of glucose-6-phosphate dehydrogenase. Deficiency of which of the following erythrocyte enzymes has the same pathophysiology as this patient’s condition? • A. bisphosphoglycerate mutase • B. pyruvate kinase • C. hexokinase • D. trans ...
... male who suffers from periodic hemolysis demonstrate a low activity of glucose-6-phosphate dehydrogenase. Deficiency of which of the following erythrocyte enzymes has the same pathophysiology as this patient’s condition? • A. bisphosphoglycerate mutase • B. pyruvate kinase • C. hexokinase • D. trans ...
Problem set answers
... This mutation could result in an increased binding affinity as evidenced by the decrease in Km. More likely, the enzyme follows steady state kinetics for which Km=k2/k1, for which a decrease in k2 (I.e., kcat) would result in a lower Km as observed. The data presented do not allow one to distinguish ...
... This mutation could result in an increased binding affinity as evidenced by the decrease in Km. More likely, the enzyme follows steady state kinetics for which Km=k2/k1, for which a decrease in k2 (I.e., kcat) would result in a lower Km as observed. The data presented do not allow one to distinguish ...
industrial biotechnology basics
... substrates, and the enzyme converts them into different molecules, called the products. products Almost all processes in a biological cell need enzymes to occur at significant rates. Since enzymes are selective for their substrates and speed up only a few g many yp possibilities,, the set of enzymes ...
... substrates, and the enzyme converts them into different molecules, called the products. products Almost all processes in a biological cell need enzymes to occur at significant rates. Since enzymes are selective for their substrates and speed up only a few g many yp possibilities,, the set of enzymes ...
Chapter 2
... -has a specific function e.g. hemoglobin –has iron ring that binds to oxygen. glycoprotein – carbohydrate (sugar) is prosthetic group. Enzymes – proteins that function as a catalyst – permit biochemical reactions to occur rapidly at normal body temperature. - they act upon substrates (other substanc ...
... -has a specific function e.g. hemoglobin –has iron ring that binds to oxygen. glycoprotein – carbohydrate (sugar) is prosthetic group. Enzymes – proteins that function as a catalyst – permit biochemical reactions to occur rapidly at normal body temperature. - they act upon substrates (other substanc ...
02.Products of Biochemical Engineering.web
... biotransformation reactions – ethanol --- acetic acid (Babylon, 5000 BC) – isopropanol --- acetone – sorbitol --- sorbose (manufacture of vit.C) – steroid transformations – fumarate --- malate ...
... biotransformation reactions – ethanol --- acetic acid (Babylon, 5000 BC) – isopropanol --- acetone – sorbitol --- sorbose (manufacture of vit.C) – steroid transformations – fumarate --- malate ...
Catalysis - University of California, Davis
... specificity of the protease used. •Transesterification* -glycosidases can reshuffle sugars •Lactase is specific for beta-galactosides •invertase is specific for beta-fructosides •Neither cares very much what the other reagent is. *(catalysts catalyze both forward and reverse reactions) ...
... specificity of the protease used. •Transesterification* -glycosidases can reshuffle sugars •Lactase is specific for beta-galactosides •invertase is specific for beta-fructosides •Neither cares very much what the other reagent is. *(catalysts catalyze both forward and reverse reactions) ...
Macromolecules biologyjunction
... 2. Enzymes can be denatured (unfolded) by what environmental factors? 3. What process is used to link amino acids together? What byproduct is produced ...
... 2. Enzymes can be denatured (unfolded) by what environmental factors? 3. What process is used to link amino acids together? What byproduct is produced ...
the ubiquitin system and a putative stimulatory role
... Among eukaryotes, ubiquitin is highly conserved, meaning that the amino acid sequence does not differ much when very different organisms are compared. Ub is a heat-stable protein that folds up into a compact globular structure. It is found throughout the cell and can exist either in free form or as ...
... Among eukaryotes, ubiquitin is highly conserved, meaning that the amino acid sequence does not differ much when very different organisms are compared. Ub is a heat-stable protein that folds up into a compact globular structure. It is found throughout the cell and can exist either in free form or as ...
Fall `94
... like carbohydrates. The most common amino acid is alanine; if it is transaminated, what product remains? __________________. How much energy, in integral ATP units, can be gained by oxidizing this product all the way to carbon dioxide and water? ______________. (SHOW WORK and STATE ASSUMPTIONS) ...
... like carbohydrates. The most common amino acid is alanine; if it is transaminated, what product remains? __________________. How much energy, in integral ATP units, can be gained by oxidizing this product all the way to carbon dioxide and water? ______________. (SHOW WORK and STATE ASSUMPTIONS) ...
Review Sheet Exam 1 C483 Spring 2014
... hierarchy of protein structure (primary-secondary-tertiary-quaternary). Understand basic motifs of protein structure and the forces that govern them. Be familiar with supersecondary structures. Be conversant with the various methods of depicting protein structures. Understand domains and the assembl ...
... hierarchy of protein structure (primary-secondary-tertiary-quaternary). Understand basic motifs of protein structure and the forces that govern them. Be familiar with supersecondary structures. Be conversant with the various methods of depicting protein structures. Understand domains and the assembl ...
A1984SR69800002
... the formation of cyanate followed by its rapid conversion to imino carbonate. The final coupling products were thought to be gels containing mixtures of imino carbonic acid esters, carbonic acid esters, and carbamate substituents, and, somewhat later, isourea linkages were also considered. Evidence ...
... the formation of cyanate followed by its rapid conversion to imino carbonate. The final coupling products were thought to be gels containing mixtures of imino carbonic acid esters, carbonic acid esters, and carbamate substituents, and, somewhat later, isourea linkages were also considered. Evidence ...
Chemical Reactions
... For a chemical reaction to take place, the reactants must collide with enough energy so that existing bonds will be broken and new bonds will be formed. If the reactants do not have enough energy, they will be unchanged after the collision. Enzymes provide a site where reactants can be brought toget ...
... For a chemical reaction to take place, the reactants must collide with enough energy so that existing bonds will be broken and new bonds will be formed. If the reactants do not have enough energy, they will be unchanged after the collision. Enzymes provide a site where reactants can be brought toget ...
All amino acids participate in these reactions at some
... All amino acids participate in these reactions at some point in their catabolism *** This is false; serine and threonine are not transaminated ¾ they are oxidatively deaminated (release NH3) by a dehydratase enzyme to form pyruvate and propionyl coA respectively. The first step in the catabolism of ...
... All amino acids participate in these reactions at some point in their catabolism *** This is false; serine and threonine are not transaminated ¾ they are oxidatively deaminated (release NH3) by a dehydratase enzyme to form pyruvate and propionyl coA respectively. The first step in the catabolism of ...
No Slide Title
... major mediator of cAMP action. PKA specifically phosphorylates serine or threonine residues preferably in the following amino acid sequence: Arg - Arg - X Ser (or Thr) - Y, ( where X is a small residue and Y is a large hydrophobic residue). Most kinases rely primarily on the amino acid sequence surr ...
... major mediator of cAMP action. PKA specifically phosphorylates serine or threonine residues preferably in the following amino acid sequence: Arg - Arg - X Ser (or Thr) - Y, ( where X is a small residue and Y is a large hydrophobic residue). Most kinases rely primarily on the amino acid sequence surr ...
Enzyme
Enzymes /ˈɛnzaɪmz/ are macromolecular biological catalysts. Enzymes accelerate, or catalyze, chemical reactions. The molecules at the beginning of the process are called substrates and the enzyme converts these into different molecules, called products. Almost all metabolic processes in the cell need enzymes in order to occur at rates fast enough to sustain life. The set of enzymes made in a cell determines which metabolic pathways occur in that cell. The study of enzymes is called enzymology.Enzymes are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Enzymes' specificity comes from their unique three-dimensional structures.Like all catalysts, enzymes increase the rate of a reaction by lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. An enzyme's activity decreases markedly outside its optimal temperature and pH.Some enzymes are used commercially, for example, in the synthesis of antibiotics. Some household products use enzymes to speed up chemical reactions: enzymes in biological washing powders break down protein, starch or fat stains on clothes, and enzymes in meat tenderizer break down proteins into smaller molecules, making the meat easier to chew.