Carbohydrates (CHO)
... compounds, however, most of animal CHO is derived from plants. The main disease associated with CHO metabolism is diabetes mellitus. ...
... compounds, however, most of animal CHO is derived from plants. The main disease associated with CHO metabolism is diabetes mellitus. ...
Enzyme Catalysis Introduction
... Enzyme Catalysis Introduction: In general, enzymes are proteins produced by living cells, they act as catalysts in biochemical reactions. A catalyst affects the rate of a chemical reaction. One consequence of enzyme activity is that cells can carry out complex chemical activities at relative low tem ...
... Enzyme Catalysis Introduction: In general, enzymes are proteins produced by living cells, they act as catalysts in biochemical reactions. A catalyst affects the rate of a chemical reaction. One consequence of enzyme activity is that cells can carry out complex chemical activities at relative low tem ...
ENZYMES
... *Each individual step is referred to as an intermediate step or an elementary process. - cellular respiration is actually made up of three stages each with multiple steps: Glycolysis ( 9 reactions), Krebs Cycle (8 reactions), Electron Transport Chain (~ 6-8 redox reactions). - a generalized metabol ...
... *Each individual step is referred to as an intermediate step or an elementary process. - cellular respiration is actually made up of three stages each with multiple steps: Glycolysis ( 9 reactions), Krebs Cycle (8 reactions), Electron Transport Chain (~ 6-8 redox reactions). - a generalized metabol ...
Enzyme Quiz # 20 First : Last: 1. Explain how an enzyme speeds up
... 2. Explain how the body is able to activate an enzyme in one part of the digestive tract (i.e stomach) and then denature the enzyme in later parts of the digestive tract ( i.e small intestine ) and at the same time activate other digestive enzymes in the small intestine to help this organ fulfill it ...
... 2. Explain how the body is able to activate an enzyme in one part of the digestive tract (i.e stomach) and then denature the enzyme in later parts of the digestive tract ( i.e small intestine ) and at the same time activate other digestive enzymes in the small intestine to help this organ fulfill it ...
Toothpickase Lab
... Active site = the fold/pocket where an enzyme’s substrate fits into. An enzyme acts only on a specific substrate because only that substrate fits into its active site. Three steps of enzyme activity: 1. A substrate attaches to an enzyme’s active site. 2. The enzyme reduces the activation energy of t ...
... Active site = the fold/pocket where an enzyme’s substrate fits into. An enzyme acts only on a specific substrate because only that substrate fits into its active site. Three steps of enzyme activity: 1. A substrate attaches to an enzyme’s active site. 2. The enzyme reduces the activation energy of t ...
Ch 31 reading guide
... 1.What is nitrogen fixation? How much ATP does it cost to form two molecuels of ammonia one molecule of N2? 2. Plants and micororganisms can incorporate ammonia into amino acids by reductive amination of a-ketoglutarate to form __________________. 3. Ammonia can also be incorporated into glutamate t ...
... 1.What is nitrogen fixation? How much ATP does it cost to form two molecuels of ammonia one molecule of N2? 2. Plants and micororganisms can incorporate ammonia into amino acids by reductive amination of a-ketoglutarate to form __________________. 3. Ammonia can also be incorporated into glutamate t ...
Enzymes - Bioclass
... d) Activated complex. The substrate is weakened to allow the reaction. e)Unchanged enzyme/ re-used at low concentrations f) Product of the reaction other keypoints from the hypothesis: ...
... d) Activated complex. The substrate is weakened to allow the reaction. e)Unchanged enzyme/ re-used at low concentrations f) Product of the reaction other keypoints from the hypothesis: ...
Questions for Enzyme - I
... a. Made up of catalytic site & substrate binding site b. Flexible in nature – changes its conformation upon substrate binding c. Specificity of enzyme resides in active site d. All of the above 7. Most accepted theory for substrate binding with the enzyme is a. Lock & key theory b. Koshlands induced ...
... a. Made up of catalytic site & substrate binding site b. Flexible in nature – changes its conformation upon substrate binding c. Specificity of enzyme resides in active site d. All of the above 7. Most accepted theory for substrate binding with the enzyme is a. Lock & key theory b. Koshlands induced ...
logcsscibap_2_4_2_c_..
... Are the shapes of the reactant and active site similar or different? Explain your answer. (2 marks) ...
... Are the shapes of the reactant and active site similar or different? Explain your answer. (2 marks) ...
Amino Acids, Proteins, and Enzymes
... • are most active at an optimum temperature (usually 37°C in humans). • show little activity at low temperatures. • lose activity at high temperatures as denaturation occurs. ...
... • are most active at an optimum temperature (usually 37°C in humans). • show little activity at low temperatures. • lose activity at high temperatures as denaturation occurs. ...
Exam 2
... C. ____________ Transition state analogues typically have lower dissociation constants for an enzyme than substrate analogues do. D. ____________ Integral proteins are reversibly anchored into the membrane. E. ____________ Symport transporters require energy input, but antiport transporters are pass ...
... C. ____________ Transition state analogues typically have lower dissociation constants for an enzyme than substrate analogues do. D. ____________ Integral proteins are reversibly anchored into the membrane. E. ____________ Symport transporters require energy input, but antiport transporters are pass ...
Bio301 Biochemistry I
... decreases) its affinity of oxygen binding. e) Carbon dioxide reacts with the amino terminal groups of hemoglobin to form carbamate groups, which carry a ______________ charge. Question 7 (5 points). A mutant hemoglobin gene has been isolated and shown to encode an abnormal a chanin by endonuclease d ...
... decreases) its affinity of oxygen binding. e) Carbon dioxide reacts with the amino terminal groups of hemoglobin to form carbamate groups, which carry a ______________ charge. Question 7 (5 points). A mutant hemoglobin gene has been isolated and shown to encode an abnormal a chanin by endonuclease d ...
Enzymes
... catalysts used by cells to initiate chemical reactions. Cells can regulate which reactions occur and how quickly by regulating which enzymes are present. ...
... catalysts used by cells to initiate chemical reactions. Cells can regulate which reactions occur and how quickly by regulating which enzymes are present. ...
Enzyme Mechanisms
... system is the ribosome. The central catalytic activity of the ribosome (peptide bond formation) is catalyzed by an RNA component. ...
... system is the ribosome. The central catalytic activity of the ribosome (peptide bond formation) is catalyzed by an RNA component. ...
Enzymes: Principles of Catalysis
... • Carry out algebra ... – ... or graph theory for complex reactions • Simplest Model Mechanism: E + S ES E + P – One reactant, one product, no inhibitors ...
... • Carry out algebra ... – ... or graph theory for complex reactions • Simplest Model Mechanism: E + S ES E + P – One reactant, one product, no inhibitors ...
Enzyme Notes
... Enzymes are specific • This means that they only work with one particular substrate. • No other substrate can fit into the active site of the enzyme. http://www.lpscience.fatcow.com/jwanamake r/animations/Enzyme%20activity.html ...
... Enzymes are specific • This means that they only work with one particular substrate. • No other substrate can fit into the active site of the enzyme. http://www.lpscience.fatcow.com/jwanamake r/animations/Enzyme%20activity.html ...
Chapter 6: An introduction to metabolism
... site ii. Noncompetitive inhibitor binds to a location (allosteric site) away from the active site but changes the conformation so that the active site does not function iii. Allosteric enzymes are usually made of multiple polypeptides and fluctuate between active forms and inactive forms iv. Alloste ...
... site ii. Noncompetitive inhibitor binds to a location (allosteric site) away from the active site but changes the conformation so that the active site does not function iii. Allosteric enzymes are usually made of multiple polypeptides and fluctuate between active forms and inactive forms iv. Alloste ...
Metabolism, Energy and Enzymes Team – Game – Tournament
... 38. Why are product molecules released from the enzyme’s active site? 39. What are the non-protein, organic molecules that assist enzymes in catalyzing a biochemical reaction? 40. What are the metal, non-organic molecules that assist enzymes in catalyzing a biochemical reaction? 41. State one of the ...
... 38. Why are product molecules released from the enzyme’s active site? 39. What are the non-protein, organic molecules that assist enzymes in catalyzing a biochemical reaction? 40. What are the metal, non-organic molecules that assist enzymes in catalyzing a biochemical reaction? 41. State one of the ...
Reading Guide for Essay Name What Happens to the Food You Eat
... Draw a large piece of food and the same piece of food chewed up into bits. Draw arrows on the chewed up food showing the increased surface area to which more enzymes can now come into contact. ...
... Draw a large piece of food and the same piece of food chewed up into bits. Draw arrows on the chewed up food showing the increased surface area to which more enzymes can now come into contact. ...
Chemical Reactions and Enzymes
... Substrate binds to the active site on the enzyme. AKA “lock and key” ...
... Substrate binds to the active site on the enzyme. AKA “lock and key” ...
Enzymes - CSUN Moodle
... Vmax [ S ] ;Vo = v= K m + [S ] K m + [S ] • kcat (turnover number): how many substrate molecules can one enzyme molecule convert per second • Km (Michaelis constant): an approximate measure of substrate’s affinity for enzyme • Microscopic meaning of Km and kcat depends on the details of the mechanis ...
... Vmax [ S ] ;Vo = v= K m + [S ] K m + [S ] • kcat (turnover number): how many substrate molecules can one enzyme molecule convert per second • Km (Michaelis constant): an approximate measure of substrate’s affinity for enzyme • Microscopic meaning of Km and kcat depends on the details of the mechanis ...
Cell Biology - smithycroft
... bind to the enzyme and react. These are the substrate molecules. The part of the enzyme to which the reactant binds is called the active site. This is a very specific shape and the most important part of the enzyme. ...
... bind to the enzyme and react. These are the substrate molecules. The part of the enzyme to which the reactant binds is called the active site. This is a very specific shape and the most important part of the enzyme. ...
THIS IS A SELF TEST - ALL THESE QUESTIONS
... 39. In humans what is the path of an oxygen molecule from the mouth to the alveoli 40. Explain what happens to an enzyme molecule when it is denatured by high temperatures. 41. Why does an enzyme only speed up one (or at the most a few) different chemical reaction(s)? 42. How do enzymes speed up the ...
... 39. In humans what is the path of an oxygen molecule from the mouth to the alveoli 40. Explain what happens to an enzyme molecule when it is denatured by high temperatures. 41. Why does an enzyme only speed up one (or at the most a few) different chemical reaction(s)? 42. How do enzymes speed up the ...
Isomerase
Isomerases are a general class of enzymes which convert a molecule from one isomer to another. Isomerases can either facilitate intramolecular rearrangements in which bonds are broken and formed or they can catalyze conformational changes. The general form of such a reaction is as follows:A–B → B–AThere is only one substrate yielding one product. This product has the same molecular formula as the substrate but differs in bond connectivity or spatial arrangements. Isomerases catalyze reactions across many biological processes, such as in glycolysis and carbohydrate metabolism.