Chapter 2 The Chemistry of Life
... 2) Create its “lock & key” substrate 3) Name your enzyme (enzyme’s end with the ...
... 2) Create its “lock & key” substrate 3) Name your enzyme (enzyme’s end with the ...
Chapter 4 Drug Biotransformation
... Subfamily - 40-55% homology of amino acid sequence; eg. CYP1A Subfamily - additional arabic numeral when more than 1 subfamily has been identified; eg. CYP1A2 ...
... Subfamily - 40-55% homology of amino acid sequence; eg. CYP1A Subfamily - additional arabic numeral when more than 1 subfamily has been identified; eg. CYP1A2 ...
Enzymes
... • Raising or lowering the pH influences the acidic and basic side chains in enzymes. Many enzymes are also denatured by pH extremes. (E.g., pickling in acetic acid [vinegar] preserves food by deactivating bacterial ...
... • Raising or lowering the pH influences the acidic and basic side chains in enzymes. Many enzymes are also denatured by pH extremes. (E.g., pickling in acetic acid [vinegar] preserves food by deactivating bacterial ...
Transport
... body of complex chemical compounds from smaller simpler compounds (e.g., proteins from amino acids), usually with the use of energy. ...
... body of complex chemical compounds from smaller simpler compounds (e.g., proteins from amino acids), usually with the use of energy. ...
Unit 3 Exam Enzymes REVIEW
... Enzyme Structure and Function (5.4 and 5.5): How do enzymes work? Why are enzymes substrate specific? Use tertiary structure of a protein to explain. What environmental factors can influence the shape of an enzyme? Explain how. Explain what the optimal environment is given the graph below. Research ...
... Enzyme Structure and Function (5.4 and 5.5): How do enzymes work? Why are enzymes substrate specific? Use tertiary structure of a protein to explain. What environmental factors can influence the shape of an enzyme? Explain how. Explain what the optimal environment is given the graph below. Research ...
Review: Thermodynamics and Cell Respiration
... 5. Define activation energy and briefly describe why it is a part of all biochemical reactions. ...
... 5. Define activation energy and briefly describe why it is a part of all biochemical reactions. ...
Patrick, An Introduction to Medicinal Chemistry 5e Chapter 3
... The Lineweaver-Burke plot has 1/initial rate on the y-axis and 1/substrate concentration on the x-axis. This should give a straight line having an intercept of 0.00400 on the y-axis and a slope of 0.00155 Therefore, the maximum rate of reaction = 1/intercept = 250.2 mol dm-3 s-1 KM = slope x (maximu ...
... The Lineweaver-Burke plot has 1/initial rate on the y-axis and 1/substrate concentration on the x-axis. This should give a straight line having an intercept of 0.00400 on the y-axis and a slope of 0.00155 Therefore, the maximum rate of reaction = 1/intercept = 250.2 mol dm-3 s-1 KM = slope x (maximu ...
Intro to Matter Intro to BioMolecules
... out test tubes into trash. Rinse out test tubes VERY well. Wash EXTREMELY WELL with dish soap and brush. Store upside down. Thank you! ...
... out test tubes into trash. Rinse out test tubes VERY well. Wash EXTREMELY WELL with dish soap and brush. Store upside down. Thank you! ...
Keshara Senanayake BIO TEST STUDY GUIDE Remember to check
... > some nucleotides have extra phosphate groups. These di/tri phosphate nucleotides such as adenosine triphosphate (ATP) are unstable molecules that carry energy >nucleotides that assist guiding chemical reactions are called coenzymes (contained in vitamins) WHAT ARE ENZYMES -Enzymes are biological c ...
... > some nucleotides have extra phosphate groups. These di/tri phosphate nucleotides such as adenosine triphosphate (ATP) are unstable molecules that carry energy >nucleotides that assist guiding chemical reactions are called coenzymes (contained in vitamins) WHAT ARE ENZYMES -Enzymes are biological c ...
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 ...
... 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 ...
(C)
... 26. What motor protein generates the sliding of microtubules that leads to bending of cilia? (A) actin, (B) myosin, (C) dynein, (D) kinesin, (E) tubulin. 27. N-acetylglutamate functions in ammonium incorporation into metabolic intermediates as: (A) a coenzyme for glutamine synthetase (GS), (B) a com ...
... 26. What motor protein generates the sliding of microtubules that leads to bending of cilia? (A) actin, (B) myosin, (C) dynein, (D) kinesin, (E) tubulin. 27. N-acetylglutamate functions in ammonium incorporation into metabolic intermediates as: (A) a coenzyme for glutamine synthetase (GS), (B) a com ...
Enzyme powerpoint
... each enzyme works with a specific substrate chemical fit between active site & substrate H bonds & ionic bonds ...
... each enzyme works with a specific substrate chemical fit between active site & substrate H bonds & ionic bonds ...
FlyCutTM XmaI - AP
... FlyCutTM XmaI is expressed and purified from E.coli that carries the recombinant XmaI gene. The molecular weight is 37.6 kDa, with the recognition site at C^CCGGG. The reaction is conducted for 5-10 minutes at 37oC, and heat-inactivated at 65oC for 20 minutes. This enzyme is not sensitive to dam or ...
... FlyCutTM XmaI is expressed and purified from E.coli that carries the recombinant XmaI gene. The molecular weight is 37.6 kDa, with the recognition site at C^CCGGG. The reaction is conducted for 5-10 minutes at 37oC, and heat-inactivated at 65oC for 20 minutes. This enzyme is not sensitive to dam or ...
Enzyme Optimum pH - Sir Sabir Hussain
... All enzymes are globular proteins (except nucleases) They increase the rate of reaction without being used up They do not affect the nature or properties of end products Small amount of enzyme can accelerate chemical reactions They are very specific in their action; a single enzyme catalyzes a singl ...
... All enzymes are globular proteins (except nucleases) They increase the rate of reaction without being used up They do not affect the nature or properties of end products Small amount of enzyme can accelerate chemical reactions They are very specific in their action; a single enzyme catalyzes a singl ...
L3 - Bacterial Metabolism v3
... • What happens as temperature increases? • What is the optimum temperature? • What would happen if you put a mesophilic organism in a thermophilic environment? ...
... • What happens as temperature increases? • What is the optimum temperature? • What would happen if you put a mesophilic organism in a thermophilic environment? ...
Bioinformatic analysis of diverse protein superfamilies to
... superfamily can be used to decipher the natural mutation patterns and their implications for protein function and stability. Positions which are conserved in a column of a multiple alignment can define general properties of the entire superfamily (for example, have direct roles in enzyme catalytic m ...
... superfamily can be used to decipher the natural mutation patterns and their implications for protein function and stability. Positions which are conserved in a column of a multiple alignment can define general properties of the entire superfamily (for example, have direct roles in enzyme catalytic m ...
REVISED Review 4 - Bonham Chemistry
... 37. Explain what is wrong with the following statement: “Enzymes shift the chemical equilibrium to more heavily favor products.” ...
... 37. Explain what is wrong with the following statement: “Enzymes shift the chemical equilibrium to more heavily favor products.” ...
Page 20-1 CHAPTER 20: Enzymes 20.2
... • Rate initially responsive to [S] • Rate eventually reaches a maximum (Vmax) ...
... • Rate initially responsive to [S] • Rate eventually reaches a maximum (Vmax) ...
Topic guide 1.2: Enzymes
... be an increased number of collisions between enzyme and substrate molecules. This in turn will increase the rate of reaction and so the products will be formed more quickly. However, applying too much heat can cause enzymes to denature. The increased vibrations and collisions put strains on the bond ...
... be an increased number of collisions between enzyme and substrate molecules. This in turn will increase the rate of reaction and so the products will be formed more quickly. However, applying too much heat can cause enzymes to denature. The increased vibrations and collisions put strains on the bond ...
Biochem 330 Fall 2011 Problem Set II Enzyme Catalysis, Glycolysis
... glyceraldehyde 3-phosphate (GAP) tritiated at C2. The dihydroxyacetone phospate (DHAP) product had lost the label at the middle carbon and showed less than 5% labelling at the C1 carbon. Which of the following is true. Explain. a) This experiment suggests that a single catalytic group on the enzyme ...
... glyceraldehyde 3-phosphate (GAP) tritiated at C2. The dihydroxyacetone phospate (DHAP) product had lost the label at the middle carbon and showed less than 5% labelling at the C1 carbon. Which of the following is true. Explain. a) This experiment suggests that a single catalytic group on the enzyme ...
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.