. What is the most prevalent anomeric form of glucose present in physiological systems?

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1967, Rabin demonstrated that a single substrate reaction catalised by an enzyme that has a single binding site for the substrate, can show sigmoidal kinetics. Discuss this scenario so that it is clear why a plot of Vo versus [SJ at fixed total enzyme concentration will be sigmoidal.

10. Consider the beta oxidation of stearic acid (C18:0): How many ATP are generated in complete oxidation of stearic acid? How many NADH are generated in complete oxidation of stearic acid? How many FADH2 are generated in complete oxidation of stearic acid?

3. One indication of the relative importance of various ATP-producing pathways is the Vmax of certain enzymes of these pathways. The values of Vmax of several enzymes from the pectoral muscles (chest muscles used for flying) of pigeon and pheasant are listed below. Vmax (umol substrate/min/g tissue) Enzyme Pigeon Pheasant Hexokinase 3.0 2.3 Glycogen phosphorylase Phosphofructokinase-1 Citrate synthase Triacylglycerol lipase 18.0 120.0 143.0 24.0 100.0 15.0 0.07 0.01 b. Compare oxygen consumption in the two birds.

5) The disease Phenylketonuria (or PKU) occurs when the enzyme that helps to catalyze the conversion of the amino acid phenylalanine into non-harmful tyrosine is mutated and doesn't work as well (or at all). Phenylalanine will still break down into tyrosine by itself, because this is a favorable reaction. Why is the non-functional enzyme a problem? Explain in a few sentences. al.H.colbe91srtihot wolsd sldu non lom i anolterineon mundillups betsmus 8880

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Predict the effect of each of the following amino acid substitutions on the KM and kcat of the enzyme-catalyzed reactions

1. Requirements of Active Sites in Enzymes The active site of an enzyme usually consists of a pocket on the enzyme surface lined with amino acid side chains necessary to bind the substrate and catalyze its chemical transformation. Carboxypeptidase, which sequentially removes the carboxyl-terminal amino acid residues from its peptide substrates, consists of a síngle chain of 307 amino acids. The two essential catalytic groups in the active site are furnished by Arg45 and Glu²7º. (a) If the carboxpeptidase chain were a perfect a-helix, how far apart (in nanometers) would Arg'45 and Glu²7º be? Hint: In an æ-helix, there is 1.5 Å translation of the backbone per residue (Chapter 3). (b) Explain how it is that these two amino acids, so distantly separated in the sequence, can catalyze a reaction occurring in the space of a few tenths of a nanometer. (c) If only these two catalytic groups are involved in the mechanism of hydrolysis, why is it necessary for the enzyme to contain such a large…

2A. Red blood cells synthesize and degrade 2,3-bisphosphoglycerate (2,3-BPG) by a detour of the glycolytic pathway, as shown below: glyeeraldehyde 3-phosphate GAP dehydrogenase 1,3-bisphosphoglycerate bisphosphoglycerate mutase ADP phosphoglycerate kinase 2,3-bisphosphoglycerate ATP 3-phosphoglycerate 2,3-bisphosphoglycerate phosphatase phosphoglycerate mutase 2-phosphoglycerate (i) The bisphosphoglycerate mutase/2,3-bisphosphoglcerate phosphatase reaction is catalyzed by a single enzyme, BPGM. At alkaline pH, BPGM favors the mutase activity while at lower pH, BPGM favors the phosphatase reaction. Use this information, along with the Bohr effect, to explain in the space below how red blood cells respond to a metabolic defect where a patient experiences chronic, elevated levels of lactic acid. I (ii) Individuals with red blood cell phosphoglycerate kinase deficiency suffer from moderate hemolytic anemia (a condition where red blood cells self-destruct before their normal lifespan). They…