Another of the six enzyme classes is which of the following?enzymes catalyze. These classes include the transferases, isomerases, and ligases.All enzymes can be categorized in one of six major classes based on the reactions theproteaseskinaseshydrolasesphosphatasesendonucleasesAn important factor that influences the rate of a biochemical reaction is thetemperature. Raising the temperature of a biochemical reaction has which effect uponthe kinetics of the reaction?a)b)c)d)e)increases the free energy of the reactantsincreases the free energy of the transition statedecreases the free energy of the reactantsdecreases the free energy of the transition statedecreases the free energy of the products

Enzyme classification: Enzymes are classified into six major classes namely hydrolases,…

Answered: Another of the six enzyme classes is…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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CH₂OH 애 H2COPO 2- ATP OH 1 애 애 어 애 The class of the enzyme catalyzing the reaction shown in this figure is a(n) Choose the one best answer. ligase 매 +ADP 매
hich of the following are advantages of quaternary structure? Choose all correct nswers 1) The genes may be for single subunits, rather than requirement for transcription and translation of giant sequences 2) Subunit construction may provide the structural basis for protein regulation 3) Multi-subunit proteins are more water soluble than single subunit proteins of the same size 4) Defects in protein synthesis may be fixed at the subunit level, rather than giant polypeptide level 5) May have multiple active sites - one on each subunit
The formation of a Schiff base in the enzymatically catalyzed decarboxylation of acetoacetate is an example of— electrostatic catalysis. proximity catalysis. covalent catalysis. transition-state catalysis. concerted acid/base catalysis.
Which of the following statements regarding enzyme catalysis is false? All options are false. Once formed, the transition state slowly proceeds to forming the product at a rate determined by cofactor binding The free energy of binding of the enzyme to the transition state is more favorable than the free energy of binding of the enzyme to the substrate The substrate and active site of the enzyme are solvated to promote enzyme-substrate interaction Once formed, the product dissociates from the enzyme after ATP hydrolysis in order to regenerate the active site
A biochemical reaction will proceed in the direction as written if: Group of answer choices H > 0. G = zero. H G > 0. G
The use of co-factors in catalysis: Cofactors Cofactor Origin: Structure: Catalytic role: Nicotinamide nucleotides Flavin nucleotides Adenosine phosphates Coenzyme A Biotin Coenzyme B12 Summaries the characteristics of co-factors using this table. Use both the textbook and other online sources such as Wikipedia to find the information. Under origin, report the precursor molecule e.g. “niacin” and also try to find the Vitamin X name for each compound, e.g. “Vitamin B3”. Under structure, identify the unique structural properties that allow each cofactor to perform the function it does Under catalytic role, indicate for which reactions are each of the cofactors important
Which of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are true
Catalysis through proximity and orientation effects involves: (select all that applies) Group of answer choices binding of acidic and/or basic groups in the binding site facilitating chemical reactions by binding substrates close to specific groups binding of substrate in specific, restrictive orientations depending on metal ions for catalysis
Enzyme Urease Chymotrypsin Alcohol Dehydrogenase Lysozyme 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)
The milieu wherein enzymes occur in vivo is dramatically different from in vitro experiments, which is often used to investigate enzyme. Give an overview of this as well as the nature of enzyme reactions in vivo. Name, in addition, the factors affecting the concentration of enzymes in vivo.
True or False Immobilization improves the stability of the enzyme. EnaLne, has a half-life of 10 days in free solution, but under identical conditions of temperature, pH, and medium composition, the measured half-life of a packed column is 30 days. The enzyme is immobilized in a porous sphere 5 mm in diameter.
Only a few amino acid residues are actually involved in catalysis in enzymes, yet enzymes are constructed of at least 100 amino acids, and often many more. Suggest some functions for the noncatalytic amino acids.

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Another of the six enzyme classes is which of the following? enzymes catalyze. These classes include the transferases, isomerases, and ligases. All enzymes can be categorized in one of six major classes based on the reactions the a) b) c) proteases kinases hydrolases phosphatases endonucleases