Which class of enzymes have sigmoid or S-shaped plots of the rate of a reaction, v, versus the substrate concentration, [S], instead of the hyperbolic curves of the Michaelis-Menten equation? transferases O holoenzymes O hydrolases allosteric enzymes ribozymes
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![Which class of enzymes have sigmoid or S-shaped plots of the rate of a reaction, v, versus the
substrate concentration, [S], instead of the hyperbolic curves of the Michaelis-Menten equation?
transferases
holoenzymes
O hydrolases
O allosteric enzymes
O ribozymes](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fb0016275-e9a1-4972-a183-517fe36ccc93%2Fd44a1ec1-c0f6-4e59-bb24-ba133f690b88%2Fkyvvjb_processed.jpeg&w=3840&q=75)
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- How Do Vitamin-Derived Coenzymes Aid Metabolism? What chemical functionality is provided to enzyme reactions by pyridoxal phosphate (we Chapter 13)? By coenzyme A (see Chapter I9)? By vitamin B12 (see Chapter 23)? By thiamine pyrophosphate (see Chapter 19)?How to differentiate the following simply by seeing the reaction: a. oxidoreductase b. transferase c. hydrolase d. lyase e. isomerase f. ligaseA generalized enzyme active site is shaped like a hemisphere with a radius of 45Å. The active site holds the following amino acids in a homeostatic solution (pH = 7.38): -HAVARILKHAVARILKHAVARILK- Assuming the charge is distributed uniformly along the hemisphere, determine the force at which this active site acts upon a single ATP molecule at the center of the hemisphere.
- The active (catalytic) site of an enzyme contains the side chains of amino acid residues that areconserved because they participate in the protein’s catalytic activity. The bulk of the enzyme,however, is not part of the active site. A substantial amount of energy is required to synthesizeenzymes. Why are these molecules so large?What are the description of the ff?A. Effect of pH with enzymaticactivity. Include example ofenzymes optimum pH.B. Effect of activators on theactivity of enzymes. Includeexamples.dipeptide + H2O → 2 amino acidsAn enzyme that catalyzes the reaction above would be called a a. hydrolase b. dehydrogenase c. lyase d. synthetase
- When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Zymogen activation Covalent modification Competitive inhibition Allosteric activation Allosteric inhibitionthe amino acid glutamic acid is at the active site of an enzyme. Normally the enzyme is active at pH 7. at pH 4 (higher concentration of H+), the enzyme is inactive. Explain there observationsEnzyme Triacylglycerol Lipase Rennin Catalase Hexokinase Enzyme Official Name (write N/A if not applicable) Enzyme Official Number (4 digits) Simple or Conjugated Enzyme (specify cofactor if applicable) Type of Reaction Catalyzed Substrate Optimum pH Optimum Temperature Function/s Disease (give 1 and describe briefly)
- An allosterically regulated enzyme in the R state is unable to bind substrate at the activesite. TrueFalsegive the properties of the enzyme (e.g., shape, size, colour, price). a) amylase b) invertaseSelect the correct option a.A holoenzyme is a catalytically inactive enzyme in the absence of its cofactor b.An enzyme cofactor is the amino acid side group in the enzyme active site c.Each of the option listed here is true d.An apoenzymes is catalytically active RNA molecule e.A co-substrate is a detachable enzyme cofactor required with another substrate for an enzyme reaction