6. Amino acid alanine containing N5 isotope in a-amino group was administratedto mouse with food. It was found that the N5 has rapidly appeared in a-aminogroups of aspartate, glutamate and other amino acids in the liver (with theexception of lysine and threonine). Explain, why does it occur? For the answer:412Chapter 8. Nitrogen metabolisma) draw the reactions of aspartate and glutamate formation with alanineparticipation;b) describe enzymes catalyzing these types of reactions; specify coenzyme;c) specify the group of amino acids due to the possibility that they have beensynthesized in the body and Glu, Ala, and Asp relate to.

The use of radioactive labelling of particular atoms have often been used to determine metabolic…

6. Amino acid alanine containing NE isotope in a-amino group was administrated to mouse with food. It was found that the N5 has rapidly appeared in a-amino groups of aspartate, glutamate and other amino acids in the liver (with the exception of lysine and threoninc). Explain, why does it occur? For the answer: Chapter 8. Nitrogen metabolism a) draw the reactions of aspartate and glutamate formation with alanine participation; b) describe enzymes catalyzing these types of reactions; specify coenzyme; c) specify the group of amino acids duc to the possibility that they have been synthesized in the body and Glu. Ala, and Asp relate to

6. Amino acid alanine containing NE isotope in a-amino group was administrated to mouse with food. It was found that the N5 has rapidly appeared in a-amino groups of aspartate, glutamate and other amino acids in the liver (with the exception of lysine and threoninc). Explain, why does it occur? For the answer: Chapter 8. Nitrogen metabolism a) draw the reactions of aspartate and glutamate formation with alanine participation; b) describe enzymes catalyzing these types of reactions; specify coenzyme; c) specify the group of amino acids duc to the possibility that they have been synthesized in the body and Glu. Ala, and Asp relate to

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 9TYK: Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric...

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The assembly of proteins from amino acids is best described as: a. a conversion of kinetic energy to potential energy reaction. b. an entropy reaction. c. a catabolic reaction. d. an anabolic reaction. e. an energy-free reaction.
In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme molecules approach maximal rate, and the substrate is continually increased, the rate of the reaction does not reach saturation. c. in the stomach, enzymes would have an optimal activity at a neutral pH. d. increasing temperature above the optimal value slows the reaction rate. e. the least important level of organization for an enzyme is its tertiary structure.
Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.
8. Match each of the following amino acids with the intermediate needed for its synthesis.(a) 3-Phosphoglycerate 1. glutamate 2. serine 3. asparagine (b) oxaloacetate 1. glutamate 2. serine 3. Asparagine
8. The chemical structure of Coenzyme A contains the following except— a phosphoanhydride moiety. a β-mercaptoethylamine residue. a lipoic acid residue. a pantothenic acid residue. an adenosine-3’- phosphate.
1. If a molecule is interating with its side chains of an enzymes active site but it is not the substrate of the enzyme what kind of enzyme regulation is this? 2. What is the change in thetype of bond between Ser 80 -> Arg. 3. Will this change cause the complex to be more or less stable. Explain
2. It is known hemoglobinopathies, whi ch arise due to mutations in one of histidines a- or B- chains binding with the iron in the heme gro up.These mutations stabilize the iron in Fes form. Some drugs (eg. sulfonamides) or chemicals( eg.anilin) also can cause methemoglobinemia. Suggest, how change the properties of Hb in these cas es. For this:1)Describe the structure and function of Hb A as a transport protein. 2) Explain the role ofiron ions in act ive centers of Hb for the binding of O23) How many molecules of Oz can bind mutant Hb, if mutation occurs in a- subunits? 4) Why can ascorbic acid be used to tr eat of such patients.
2. A mixture of the following amino acids (glu, leu, val, arg, ser, phe) was obtained upon complete hydrolysis of a hexapeptide. a. Edman’s reagent releases leucine b. Hexapeptide with carboxypeptidase releases serine. c. Hexapeptide with trypsin forms a tripeptide A with leucine at the N terminal and tripeptide B with valine at the N terminal. d. Tripeptide A with carboxypeptidase releases arginine and a dipeptide with glutamic acid at C terminal. e. Tripeptide B with chymotrypsin form releases serine and another dipeptide. Give: 1. the amino acid sequence of tripeptide A and B. 2. the amino acid sequence in the above hexapeptide.
1.One of the main sources of sphingosine in the body is in the cell membrane. What complication could arise from the biological synthesis of ceramide?
3. One of the triacylglycerols found in corn oil contains palmitic acid, linoleic acid, and linolenic acid. During the production of spreadable margarine, all of the double bonds in this triacylglycerol are converted from cis to trans isomers. Linoleic acid: CH3(CH2)4CH=CHCH2CH=CH(CH2)7COOHLinolenic acid: CH3CH2CH=CHCH2CH=CHCH2CH=CH(CH2)7COOH Palmitic acid: CH3(CH2)14COOH a. Identify the unsaturated fatty acid(s) listed above and provide the associated omega designation. b. Draw an accurate representation of the structure of the triacylglycerol present in spreadable margarine. Circle all ester bonds in the structure you have drawn.
1)Catalase a. Is catalase activity endothermic or exothermic? b. What classification of enzyme is catalase? c. Give the Enzyme Commission (E.C.) number of catalase. d. Is catalase reusable? answer all and don't copy from other sources I will downvote for sure
Nitrogen fixation is a difficult process because nitrogen exists in the atmosphere primarily as its oxides which are very unreactive O of the high polarity of nitrogen molecules preventing them from dissolving in biological fluids, such as those inside cells I O there is so little nitrogen in the atmosphere of the extreme toxicity of nitrogen O nitrogen is very unreactive, largely due to its triple bond