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Concept explainers
(a)
Interpretation: To determine the two reactants used in the further processing of glutamate via a glutamate-oxaloacetate transamination.
Concept introduction: Transamination reaction is a biochemical reaction that involves the transfer of an amino group. In transamination reaction exchange of an amino group from an
(b)
Interpretation: To determine the two products produced in the further processing of glutamate via a glutamate-oxaloacetate transamination.
Concept introduction: Transamination reaction is a biochemical reaction that involves the transfer of an amino group. In transamination reaction exchange of an amino group from an
(c)
Interpretation: To determine the type of enzyme needed in the further processing of glutamate via a glutamate-oxaloacetate transamination.
Concept introduction: Transamination reaction is a biochemical reaction that involves the transfer of an amino group. In transamination reaction exchange of an amino group from an
(d)
Interpretation: To determine the product that becomes the “nitrogen carrier” for further reactions produced in the further processing of glutamate via a glutamate-oxaloacetate transamination.
Concept introduction: Transamination reaction is a biochemical reaction that involves the transfer of an amino group. In transamination reaction exchange of an amino group from an
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Chapter 26 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- Given the following statements, identify which are true and which are not. (1) Two ribose subunits are present in the coenzyme flavin adenine dinucleotide. (2) In the common metabolic pathway, 10 molecules of ATP are produced per acetyl CoA catabolized. (3) The purpose of step 2 in the CAC is to convert a secondary alcohol to a tertiary alcohol.arrow_forwardWhich class of enzymes catalyzes the following reactions? CH2- CH2- CH2 H2- C- CH2 AST CH2-C CH2 CH-NH + C=O + C=0 + CH-NH ČO0 Čo0 ČO0 ČO0" Aspartate Oxoglutarate Oxaloacetate Glutamate Select one: a. Oxidoreductase O b. Isomerase O c. Ligase d. Transferasearrow_forwardFatty acids are converted to their coenzyme A esters in a reversible reaction catalyzed by acyl-CoA synthetase: R-COO +ATP +COA R-C-COA +AMP + PPi a) The reaction involves two steps the first of which forms an enzyme-bound intermediate identified as the mixed anhydride of the fatty acid and AMP: R-C-O-P-O-nibose-adenine Write two chemical equations coresponding to the two steps of the reaction catalyzed by the synthetase. b) The acyl-CoA synthetase reaction as written above is readily reversible. How might the reaction be made to favor formation of fatty acyl-CoA? Write within the box. Anything outside the box will not be graded. From thearrow_forward
- The PDH complex is a logical point of regulation in metabolism, as it links two major catabolic processes. Answer the following regarding the complex: a) Explain the advantage of E1, E2 and E3 working as a complex as opposed to separately. b) Explain the purpose of each of the three enzymes and their associated cofactors. c) NADH can inhibit the PDH complex directly or indirectly. What is the purpose of inhibition by NADH? d) Explain the differences between direct and indirect inhibition by NADH. Be sure to indicate the components involved and the mechanism of inhibition (impact on target component).arrow_forwardConsider the hypothetical reaction plot of salivary α-amylase shown below: a. Determine whether the plot describes substrate disappearance or product formation. Using Equation 5-2, express the rate of reaction described by the plot.b. Based on the plot, determine the time interval at which the rate of reaction must be measured.arrow_forwarda) Based on the data shown in the image, what are the Km and Vmax for the enzyme with L-DOPA and D-DOPA? Show any relevant analyses or calculatins you did to determine these values. ( HINT a graph might be helpful here! ) b) Based on your answer to part a, briefly describe how the kinetics of the enzyme differs for the two substrates. Which Substrate has better binding affinity to the enzymearrow_forward
- For the following enzymes (3-6) predict how the conditions will most likely affect the enzymes activity with one of the following and provide a 1 sentence explanation: a. increase activity b. decrease activity c. not likely to alter activity 3) alpha-ketoglutarate dehydrogenase complex binding to AMP when [AMP] is high. 4) phosphohexose isomerase binding NADH when [NADH] is high 5) phosphofructose-1 binding NAD+ when [NAD+] is high 6) pyruvate dehydrogenase complex binding to ATP when [ATP] is higharrow_forwardBecause of the position of arsenic in the periodic table, arsenate (Aso ) is chemically similar to inorganic phosphate and is used by phosphate- requiring enzymes as an alternative substrate. Organic arsenates are quite unstable, however, and spontaneously hydrolyze. Arsenate is known to inhibit ATP production in glycolysis. Identify the target enzyme, and explain the mechanism of inhibition.arrow_forwardRegarding phosphofructokinase, which of the following statements is true: a. Low [ATP] stimulates the enzyme, but fructose-2,6-bisphosphate inhibits. b. High [ATP] stimulates the enzyme, but fructose-2,6-bisphosphate inhibits. c. The enzyme is more active at low [ATP] than at high, and fructose-2,6-bisphosphate activates the enzyme. d. High [ATP] stimulates the enzyme, and fructose-2,6-bisphosphate activates.arrow_forward
- The conversion of glutamate to alpha-ketoglutarate is an example of oxidative deamination. Give the complete chemical equation of the said pathway. What happens to the second product of this reaction?arrow_forwardThe mechanism of chymotrypsin is used as a model for studying enzyme reaction mechanisms. Answer the following questions related to chymotrypsin: 1. List the 3 amino acids in the catalytic triad of chymotrypsin. 2. List the types of catalytic mechanisms (from the 3 main types of catalytic mechanisms) displayed in the mechanism of chymotrypsin.arrow_forwardDefine beta-oxidation of fatty acids? Describe in detail three different steps of beta-oxidation of FAs.arrow_forward
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