one way of expressing the rate at which an enzyme can catalyze a reaction is to...
one way of expressing the rate at which an enzyme can catalyze a reaction is to give its turnover number. the turnover numver is the maximum number of substrate molecules that can be acted on by one molecule of enzyme per unit of time. the following table gives the turnover number of some representative enzymes.
Enzyme: Ribonuclease (substrate RNA & Turnover number per second is 100)
Enzyme: Fumarase (substrate Fumarate & turnover number per second is 800)
Enzyme: Lactate Dehydrogenase (substrate Lactate & turnover number per second is 1000)
Enzyme: Urease (substrate Urea & turnover number per second is 10,000)
HOW MANY MOLECULES OF LACTATE CAN ONE MOLECULE OF LACTATE DEHYDROGENASE ACT ON IN 29 MINUTES?
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one way of expressing the rate at which an enzyme can catalyze a reaction is to...
help onthese 2 One way of expressing the rate at which an enzyme can catalyze a...
help onthese 2
One way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover number is the maximum number of substrate molecules that can be acted on by one molecule of enzyme per unit of time. The table gives the turnover number of four representative enzymes. Enzyme Substrate Turnover number (per second) Ribonuclease RNA 100 Fumarase fumarate 800 Lactate dehydrogenase lactate Urease urea 10,000 1000 How many molecules of...
Which of the diagrams illustrates the way in which the rate of an enzyme-controlled reaction depends...
Which of the diagrams illustrates the way in which the rate of an enzyme-controlled reaction depends on substrate concentration? * А B Rate of reaction MÚN Substrate concentration A B D When starch and amylase are mixed in the presence of iodine solution, the blue-black colour rapidly disappears. This is due to the formation of which molecule? * glucose O glycogen sucrose O maltose Which of the following enzyme groups can catalyse oxidation reactions? * O phosphorylases isomerases hydrolases dehydrogenases...
All of the following statements about the specificity constant of an enzyme are true except which...
All of the following statements about the specificity constant of an enzyme are true except which one? It is specific to a certain substrate. It is equal to ratio kcat/Km for the substrate, It is equal to the number of times an enzyme can catalyze a reaction per second. It has a maximum value around 10^8 - 10^9 /Ms, at which it is effectively limited by diffusion of the substrate to the active site
Can someone quick answer/check these questions? Thank you, will rate! (the answers that I have came...
Can someone quick answer/check these questions? Thank you, will rate! (the answers that I have came up with are in bold) Please help 51- Glycogenesis involves the following steps a) isomerisation b) activation c) elongation or coupling d) branching e) all of the above 52 During the breakdown of glycogen, free glucose is formed from A. the reducing end. B. the non-reducing end. C. glucose residues in an a 1-->4 linkage to the chain. D. glucose residues in an...
biochemistry if you could please help me answer the following questions! * 1. (5 pts) Which...
biochemistry
if you could please help me answer the following questions!
* 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
Question 89 Gluconeogenesis is the A) Result of amylase activity B) Formation of glycogen C) Formation...
Question 89 Gluconeogenesis is the A) Result of amylase activity B) Formation of glycogen C) Formation of starches D) Formation of glucose from simple two and three-carbon precursors Question 90 The only known regulatory mechanism for pyruvate carbora A) Activation by acetyl Co4 B) Activation by phosphorylation C) Activation by CAMP D) Activation by NADH 20 5 Question 87 Isozymes are enzymes A) From one species that catalyze the same reaction B) From different species that catalyze the same reaction...
2. hypothesize the best conditions (pH and temperature) under which the enzyme chymotrypsin functions with an...
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
ch 14 answer each of these. answer all 3 please HI HCI reactants Reaction intermediates are...
ch 14 answer each of these.
answer all 3 please
HI HCI reactants Reaction intermediates are species that are formed in one step of a mechanism and consumed in another step. For example, can act as an intermediate in the following reaction: H2(g) + 2Cl(g) + 2HCl(g) + 12(g). You can often express the concentration of in terms of the concentrations of the of the overall reaction to be consistent with the experimentally observed rate law as the overall reaction...
1. Which of the folowing statements about glucokinase and hexokinase (that catalyze the same reaction) is...
1. Which of the folowing statements about glucokinase and hexokinase (that catalyze the same reaction) is TRUE? A. Glucokinase has a higher capacity than hexokinase to convert glucose to glucose 6 phosphate B. Hexokinase is only active in the liver where it can utilize multiple hexoses C. While glucokinase requires ATP for its action, hexokinase requires GTP D. Glucokinase can act on multiple glucose-like sugars (such as galactose) E. Hexokinase has a higher Km and easily handles all the glucose...
Match the term to the correct description. Choices may only be used once. Group of...
Match the term to the correct description. Choices may only be used once. Group of answer choices [ Choose ] An inhibitor molecule binds to the active site. Part of an enzyme where the substrate binds to Protein molecules that function as biological catalysts An inhibitor molecule binds to an allosteric site and prevents the substrate from binding to the active site. A substance...
help onthese 2
One way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover number is the maximum number of substrate molecules that can be acted on by one molecule of enzyme per unit of time. The table gives the turnover number of four representative enzymes. Enzyme Substrate Turnover number (per second) Ribonuclease RNA 100 Fumarase fumarate 800 Lactate dehydrogenase lactate Urease urea 10,000 1000 How many molecules of...
Which of the diagrams illustrates the way in which the rate of an enzyme-controlled reaction depends on substrate concentration? * А B Rate of reaction MÚN Substrate concentration A B D When starch and amylase are mixed in the presence of iodine solution, the blue-black colour rapidly disappears. This is due to the formation of which molecule? * glucose O glycogen sucrose O maltose Which of the following enzyme groups can catalyse oxidation reactions? * O phosphorylases isomerases hydrolases dehydrogenases...
All of the following statements about the specificity constant of an enzyme are true except which one? It is specific to a certain substrate. It is equal to ratio kcat/Km for the substrate, It is equal to the number of times an enzyme can catalyze a reaction per second. It has a maximum value around 10^8 - 10^9 /Ms, at which it is effectively limited by diffusion of the substrate to the active site
biochemistry
if you could please help me answer the following questions!
* 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
Question 89 Gluconeogenesis is the A) Result of amylase activity B) Formation of glycogen C) Formation of starches D) Formation of glucose from simple two and three-carbon precursors Question 90 The only known regulatory mechanism for pyruvate carbora A) Activation by acetyl Co4 B) Activation by phosphorylation C) Activation by CAMP D) Activation by NADH 20 5 Question 87 Isozymes are enzymes A) From one species that catalyze the same reaction B) From different species that catalyze the same reaction...
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
ch 14 answer each of these.
answer all 3 please
HI HCI reactants Reaction intermediates are species that are formed in one step of a mechanism and consumed in another step. For example, can act as an intermediate in the following reaction: H2(g) + 2Cl(g) + 2HCl(g) + 12(g). You can often express the concentration of in terms of the concentrations of the of the overall reaction to be consistent with the experimentally observed rate law as the overall reaction...
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