Hi Decide whether each of the following statements is true about oxaloacetate decarboxylase.If you were to write a chemical equation for certain biochemical reactions of oxaloacetate, oxaloacetatedecarboxylase would appear only on the left-hand side.It's an enzyme, and oxaloacetate is its substrate.It has no effect on the rate at which oxaloacetate is converted to other substances.It's made by a ribosome out of amino acids.O trueO falseO trueO falseO trueO falseO trueO false

Oxalo acetate decarboxylase( OAA decarboxylase ) is an enzyme that catalyses the conversion of…

Answered: Decide whether each of the following…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter23: Fatty Acid Catabolism

Section: Chapter Questions

Problem 21P: Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved...

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Most individuals with genetic defects in oxidative phosphorylation are found to have relatively high concentrations of alanine in their blood. how this in biochemical terms? please help :)
Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess uses gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student searcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO hich uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the neweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table Table 1. Enzyme Kinetic Data Velocity, mM/s Kmp 0.0351 [S], mM Cha Хan 0.492 0.0678 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 Enzyme Kinetic Parameter: Parameters Vmax |Ku | Type of Inhibition Mode of Binding Xanthine Kaempferol Chlorogenic acid NA NA Line Weaver Burk Plot:
The 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.
True False Glucose oxidase can be used in determining glucose in the blood and urine Regardless of the distance between the enzyme and substrate, they will bind. Lipase is an enzyme primarily produced by the pancreas that breakdown peptide bonds between the oxygen molecules of glycerol and the hydroxyl molecules of fatty acids. Coenzymes are organic substances, while cofactors are inorganic. L-Amino-acid oxidase will catalyze reactions of D (-) - glycine. Redox reaction via oxidoreductase is still possible with one reactant only. The apoenzyme is the protein part of the enzyme, which is enzymatically inactive without cofactors. Lack of enzymes will lead to block in metabolic pathways causing inborn errors of metabolism Ligases are enzymes that catalyze the breakdown of chemical bonds. Ribozymes are catalytically active RNA molecules or RNA-protein complexes
Because 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.
There is another class of aldolase enzymes known as Class II. These enzymes are found in fungi, algae, and some bacteria. This class differs for Class I in that these enzymes do not have a Lys residue associated with their active sites, but contain a divalent cation (usually Zn2+ or Fe2+) in the active site. Outline a possible mechanism for a Class II aldolase and explain the function of the metal ion in the reaction.
Lactate can be converted into pyruvate by the enzyme lactate dehydrogenase and the coenzyme NAD+. Write the reaction in the standard biochemical format, using a curved arrow to show the involvement of NAD+.
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 high
In the beta oxidation of linoleic acid, converting the 3, 5, 8 trienoyl CoA intermediate back to an expected intermediate for a beta oxidation substrate costs the equivalent of how many ATPs? (hint: look at the 'right side' of the figure for addressing problem 3 with linoleic acid)
In relation to Carbamoyl Phosphate Synthetase enzyme, answer the following: A- What are the two isoforms of this enzyme, explain why there are two isoforms? B- What are the clinical manifestations associated with the deficiency of these two enzymes? C- Write down the biochemical reaction and the name of the metabolic pathway that these two isoforms are involved in, and how many ATP is utilized by these two isoforms?
Because of the position of arsenic in the periodic table, arsenate (AsO43- ) is chemically similar to inorganic phosphate and is used by phosphaterequiring 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.
Which of the following statements is true about the chymotrypsin reaction? 1. The catalytic triad at the active site is formed by three residues: His, Gly, and Ser 2. When the substrate is p-Nitrophenylacetate, the rate-limiting step is the release of p-Nitrophenolate. 3. During the reaction, LBHB forms when the proton is donated to His from Ser or water. 4. The chymotrypsin reaction involves “only” specific acid-base catalysis 5. The “oxyanion hole” is formed by the amide nitrogens of Ser and Glu

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