Understanding Browning of Fruits and Vegetables by an Enzyme 2019

Modified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true. The reaction involving the substrate bound to the active site of an enzyme is made more favorable by increasing the activation energy of the reaction.

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MULTIPLE CHOICE - Please answer properly QUESTION : Enzymes can be regulated in a many different ways. Covalent modification is one way. Here, the functional groups are attached to or removed from the enzyme. A phosphate group is an example of a functional group that can be added to an enzyme. Depending on the enzyme, addition of a phosphate group can either increase or decrease an enzyme's activity. Evaluate the following names and identify the general name of an enzyme that functions to add phosphate groups to its substrate? A. isomerase B. phosphatase C. kinase D. ligase

Why would an enzyme no longer function once it denatures?

BIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : If a cell has an adequate supply of adenine nucleotides but requires more guanine nucleotides for protein synthesis: 1. Glutamine-PRPP amidotransferase will not be fully inhibited 2. AMP will be a feedback inhibitor of the condensation of IMP with  aspartate 3. ATP will stimulate the production of GMP from IMP 4. ATP will inhibit nucleoside diphosphate reductase. Choices A. 2 and 4 B. 1 and 3 C. 1, 2, 3, and 4 D. 1, 2, and 3

Modified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true. Extreme temperatures and pH can cause permanent disruption of the protein primary structure(s) of enzymes that leads to loss of active site shape, loss of binding efficiency and activity.

Select all that apply. Which of the following are not properties of enzymes? not required to sustain the life of an organism sensitive to pH and temperature of their environment able to interact with all compounds or substrates large proteins with a special surface pattern

X Incorrect. Suppose that an uncatalyzed reaction is spontaneous because AG has a value of -10 kcal/mol. An enzyme that catalyzes the reaction is identified. What effect will the enzyme have on the rate of the reaction? Choose all that are correct. The enzyme increases the AG value. The enzyme increases the rate of reaction. The enzyme decreases the rate of reaction. The enzyme decreases the AG value. The enzyme raises the activation energy. The enzyme lowers the activation energy.

Drag and drop from the available list of terms. are a diverse set of enzyme that catalyze two molecules by forming a new bond in the process. Transferases Kinases joining Lyases Ligases separating Oxidoreductases Dehydrogenases converting hydrolytic

Question #1: Choanoflagelletes are a unicellular ancestor to animals. One observation to support this hypothesis is the appearance of adhesion molecules that are key to the development of multiceullarity. Bulk transport Gap junctions Animals. Adhesion, cell signaling Single-celled :} Insects, mammals, and other animals with bilateral symmetry (~10,000,000) Jellyfish and their relatives (10,000) } Sponges (10,000) Choanoflagellates (150) Despite their simple unicellular lifestyle they express adhesion molecules including cadherins and lectins (King et al., 2003) but don't seem to have molecules that are typically found in the extracellular matrix such as integrins or laminins (Williams et al., 2014). Design a microscopy experiment to test the assertion that choanoflagellates have (some) adhesion molecules and those molecules play a similar role in a closely related animal like sponges.

Kinetics of enzymatic reactions: the dependence of the reactionrate on the concentration of enzyme and substrate, рН andtemperature. Kinetics of allosteric enzymes

MAKE A GRAPH FOR ME ON GRAPH PAPER CALL IT ENZYMES VS RATE OF REACTION USING TABLE BELOW  GRAPH paper INSERTED BELOW rules: data points must be an x or circled dot, must be on grid paper , the independant variable on the x  axis and dependant variable on the y axis, must include titles Regarding the data points: - H2O2 + MnO2 Control #1: (Control #1, 5)- H2O2 + sand control #2: (Control #2, 0)- Plant versus Animal Liver Catalase: (Liver, 4)- Potato: Plant vs. Animal Catalase: (Potato, 3)- Substance Enzyme Concentration (Used Liver): (Liver Used, 4)- Substance Enzyme Concentration (Used H2O2): (Used H2O2, 1) - Boiling Water Bath Temperature: (Boiling Water Bath, 5)- Ice Water Bath Temperature: (Ice Water Bath, 2)- HCl, or pH 3: (H 3, 4)- NaOH at pH 12: (pH 12, 2)- pH 7 (H2O): (assuming average of pH readings; pH 7, not specified) The following explains how to display the graph: Title: Factors versus Enzyme Activity Rate - Labels on X- and Y-axes: Factors and Rate of Enzyme…

I. Active site analysis. Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid architecture of an active site is designed to bind substrates. Amino acid side chains are capable of hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0 a.a.#1 a.a.#2 a.a.#6 HO Lond NH₂ НО a.a.#5 OH a.a.#3 a.a.#4

BIOMOLECULES - MULTIPLE CHOICE - Please answer properly QUESTION : Which of the following best describes the transition state of a catalyzed reaction? A. higher in energy than that of an uncatalyzed reaction B. lower in energy than that of an uncatalyzed reaction C. bound very weakly to the catalyst D. lower energy than the reaction substrate

How enzymes works on Apple source. I need full explanation for this question.

Modified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true. The Michaelis-Menten Constant (Km) of an enzyme is equal to the enzyme concentration at which the initial velocity of the reaction is one half of maximum velocity (Vmax).

The number 2 question. Thank you

. Recall your study of equilibria and kinetics from general chemistry. You used equations with upper case Kand lower case k during the study of equilibria and kinetics respectively. What do the upper and lower case letters refer to?

multiple choice, choose the correct answer Under which of the following conditions would an enzyme fail to be accurately described by the M-M equation:1. kcat >> k1 or k-12. In the presence of a negative allosteric effector3. At low concentrations, the reaction is first order with respect to substrate concentration4. At high concentrations the reaction is zero order with respect to substrate

Enzyme-substrate complex Enzyme What concept does this picture illustrate? 4° structure hydrogen bonding Enzyme activity as a function of substrate concentration Enzyme catalysis by proximity and orientation Induced-fit model of substrate binding Lowering of activation energy barrier

choices for first blank (protonater,deprotonated) 2nd blank (higher,lower,same) 3rd blank (10,50,90,100) 4th blank (allowed from, excluded in)

dits description. Each term can only be used once. ( Choose] [Choose) on induced fit the free energy of activation, or aclivation energy nds. substrates enzyme-substrate complex on enzyme active site d its description. Each term can only be used once. Chioie pimagepeg

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Metabolic Classification What type of metabolic reaction is shown by the following reactions? Choices: Amphibolic Anabolic Catabolic

Only typed explanation

Help with the wrong ones please

Serine protease enzyme mutation   To show differences in the effect of the nucleophilic attack of the carbonyl group (C=O) of peptide bond between the catalytic triad of serine, histidine and aspartic acid, and another catalytic triad contains alanine, histidine and aspartic acid   Provide/ draw an example of catalytic mechanism with catalytic triad contains alanine, histidine and aspartic Please answer completely will give rating surely

not sure which ones apply

Fill in the blanks (write answers only in correct sequence). When the activation energy required is less between the reactants and the products, reaction is known as----- i. ii. The region of an enzyme where substrate molecules bind and undergo a chemical 11. reaction is known as--- 11. To produce amino acids and synthesis of NADH, cycle used is-- Metabolic cycle that takes place both in cytoplasm and mitochondria is--- Glucose 1 phosphate is converted to Glucose 6 Phosphate by the action of - Which vitamin deficiency is linked with the night blindness? Name it iv. V. vi.

Remember for T/F questions, either answer TRUE or FALSE, but if the answer is FALSE make sure to explain WHY the answer is false. A metabolic pathway can have unfavorable reactions within the pathway as long as the total sum of all reactions are favorable. $$ S OiLearn Video W

Graph B above depicts Lineweaver-Burk double reciprocal plot for an enzyme catalyzed reaction carried out in the presence or absence of an inhibitor. Which of the following statement best describes the kinetic data shown below: ?         Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor.       Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor.       Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor.       Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor.

helping tags: Biochemistry, spectrophotometric analysis, enzyme, substrate, coenzyme Will upvote, just pls help me create the graph. Thanks.