BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
9th Edition
ISBN: 9781319425746
Author: BERG
Publisher: MAC HIGHER
expand_more
expand_more
format_list_bulleted
Question
Chapter 9, Problem 5P
Interpretation Introduction
Interpretation:
An explanation corresponding to the fact that the mutation of the proton-shuttle residue His
Concept introduction:
Mutation is defined as the change in the sequence/order of DNA bases. It occurs due to the introduction of radiation, chemicals, or an internal disorder. Mutation may be caused by a single change in base sequence.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Instructions.
Given each set of information which may include common name(s) and the reaction catalyzed, you are required to identify the main class of the specific enzyme described.
Name: citryl-CoA synthetase
Reaction: ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA
Name: D-xylulose reductase
Reaction: xylitol + NAD+ = D-xylulose + NADH + H+
Name: cellobiose phosphorylase
Reaction: cellobiose phosphate = α-D-glucose 1-phosphate + D-glucose
Name: carbonic anhydrase
Reaction: H2CO3 = CO2 + H2O
Other info: The enzyme catalyzes the reversible hydration of gaseous CO2 to carbonic acid, which dissociates to give hydrogencarbonate above neutral pH.
Name: pantoate activating enzyme
Reaction: ATP + (R)-pantoate = AMP + diphosphate + (R)-pantothenate.
Please ASA. Thanku.
In the reaction Na + Cl à Na+ + Cl-, which component is said to become ‘oxidized’ and which is considered reduced?
Na, Cl
Cl, Cl
Na, Na
Cl, Na
Substituent effects. What is the pHPpH of a 0.1 M0.1 M solution of
chloroacetic acid (CICH2 COOH, pKa=2.86)?
(CICH, COOH, pK, = 2.86) ? do
Chapter 9 Solutions
BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
Knowledge Booster
Similar questions
- not true about the Michaelis-Menten equation? The equation that gives the rate, v, of an the substrate concentration [S] is the Michaelis-Menten equation = Vmax[S]/(Km + [S]), where V, enzyme-catalyzed reaction for all values of max and Km are constants. Which of the following is a) for [S] << Km, V = Vmax applies to most enzymes, but allosteric enzymes have different kinetics when [S] = Km, then v = Vmax/2 gives the rate when the enzyme concentration, temperature, pH, and ionic strength are constant for very high values of [S], v approaches Vmax e) Which is correct about the constant Km in the Michaelis-Menten equation? also called the catalytic constant or turnover number equal to the number of product molecules produced per unit time when the enzyme is saturated with substrate it is the constant in the first order rate equation v = k[A] it is the constant in the second order rate equation v = equal to the substrate concentration at which the velocity or rate of a reaction is ½ the…arrow_forwardENZYME KINETICS ANALYSIS of 6 Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess causes gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student researcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO which uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the Lineweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table 2 and paste a copy of your Lineweaver-Burk plot. submit the picture of your output in PNG or JPG format. Table 1. Enzyme Kinetic Data Velocity, mM/s [S], mM Хan Kmp Cha 0.492 0.0678 0.0351 0.0615 0.211 0.0531 0.0261 0.0451 0.087 0.0298 0.0157 0.0211 0.048 0.0195 0.0091 0.0142 0.029 0.0127 0.0067 0.0081 Table 2. Enzyme Kinetic Parameters Xanthine Kaempferol Chlorogenic acid Parameters Vmax Км Type of Inhibition Mode of Binding NA NA Lineweaver-Burk Plotarrow_forwardEnzymes catalyze chemical reactions. What constitutes the active site of an enzyme? What are the turnover number (kcat), the Michaelis constant (Km), and the maximal velocity (Vmax) of an enzyme? The kcat (catalytic rate constant) for carbonic anhydrase is 5 × 105 molecules per second. This is a “rate constant,” but not a “rate.” What is the difference? By what oncentration would you multiply this rate constant in order to determine an actual rate of prod- uct formation (V)? Under what circumstances would this rate become equal to the maximal velocity (Vmax) of the enzyme?arrow_forward
- 1. pH Effects a. In the enzyme mechanism of lysozyme, two acidic amino acid residues, Asp52 and Glu35, are critical for catalytic activity. If we assume normal side chain pKa values for Asp (pKar = 3.90) and for Glu (pKar = 4.07), what proportion of enzyme molecules will have both Asp52 and Glu35 in the correct ionization state at pH 5.0 (the pH optimum for lysozyme)? b. Are the traditional pKa values likely to be correct within the protein? What pKa changes might be present within lysozyme?arrow_forwardSynthetic stoichiometries. What is the stoichiometry of the synthesis of... (a) ribose 5-phosphate from glucose 6- phosphate without the concomitant generation of NADPH? (b) NADPH from glucose 6-phosphate without the concomitant formation of pentose sugars?arrow_forwardSelect all that apply. What is true about the conformational aspects of coupling? O The proton gradient is involved in the release of bound ATP from the synthase as a result of conformational change. O The conformational states interconvert as a result of proton flux through the synthase. There are two sites for substrate on the synthase and two possible conformational states: open (0) and tight-binding (T). Dinitrophenol binds to and inhibits ATP synthase conformational changes, thus inhibiting ATP synthesis. The Fo portion of ATP synthase acts as a rotary motor.arrow_forward
- For 100 words. What are the two essential requirements to effectively carry out metabolic work?arrow_forwardMore ratios. Through the use of nuclear magnetic resonance spectroscopy, it is possible to determine the ratio between the protonated and deprotonated forms of buffers. (a) Suppose the ratio of [ A- ]A I to [HA] is determined to be 0.1 for a buffer with pKar6.0.pKa = 6.0. What is the pH? (b) For a different buffer, 91974 suppose the ratio of [ A- ]lA J to [HA] is determined to be 0.1 and the pHpH is 7.0. In this case, what is the pKapKa of the buffer? (c) For another buffer with pKa=7.5PKa = 7.5 at pH 8.0pH 8.0, what is the expected ratio of [ A- ][A ] to [HA]? doarrow_forward. Pyruvate can be processed under anaerobic conditions to ethanol (in yeast) or to lactate (in mammals), as shown. Explain the primary purpose of these reactions. Describe the major biochemical features of each reactionarrow_forward
- Detailed with reactions.Why does FAD accepts 2 protons in dehydration of succinate to fumarate? Why dont NAD molecules participate in this reaction?arrow_forwardOH affromah. The Standard free energy CAGO¹) of the reaction shown above can be estimated based on? OH A. High Energy bands B. Reduction potential C. cannot be estimated OH energy. он The reaction shown above requires the cofactor to proceed forward without significant was te of A.ATP B. Nicotinamide C. Flavin D. No cofactor required 3 Determine approximate 46°1 of the coupled reaction KJ/mol possible answers: (0,-8,-15,-22,-30, -38,-45) The class of enzyme that catalyzes the reaction is possible answers: Mutase, Isomerase, ki nase, phosphatase, Dehydrogenase, Aidolasearrow_forwardBIOCHEMISTRY DRAWING. pls accept question only if 100% confident please and thank you. Enalapril is inactive until acted upon by an esterase. Draw the structure of the resulting bioactive derivative. Hintarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning