One of the enzymes in glycolysis is aldolase, which requires Zn" for catalysis. Under conditions of Zn deficiency, when the enzyme lacks zinc, it would be referred to as:
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- Human blood serum contains a class of enzymes known as acid phosphatases, which hydrolyze biological phosphate esters under slightly acidic conditions (pH 5.0): R-O-P-O3-2 + H2O --> R-OH + HO-P-O3-2. Acid phosphatases are produced by erythrocytes, the liver, kidney, spleen, and prostate gland. The enzyme from the prostate gland is clinically important because an increased activity in the blood is frequently an indication of cancer of the prostate gland. The phosphatase from the prostate gland is strongly inhibited by tartrate ion, but acid phosphatases from other tissues are not. How can this information be used to develop a commercial specific procedure for measuring the activity of the acid phosphatase of the prostate gland in human blood serum? * 1. Prostate cancer cannot be diagnosed biochemically. 2. Use tartrate to inhibit phosphatase from prostate gland and then subtract the results from the total serum enzyme activities to get an…In Bacillus subtilis, threonine is metabolized by the following sequence of reactions: (a) oxidation; (b) decarboxylation;(c) transamination; and (d) oxidation to produce pyruvate. Outline this sequence of steps, show the structures of thesubstances, use abbreviations for the cofactors, and show any enzyme-bound coenzymes. What type of enzyme bound intermediate is likely for reaction (d)?A glycolytic intermediate may be used to make the glycerol 3-phosphate necessary for the production of glycerophospholipids. For this conversion, provide a reaction sequence.
- The active site of an enzyme that uses a general acid-base catalytic mechanism contains a Glu and an Asp residue (both of which are essential for catalysis) with pKa values of 5.9 and 4.5, respectively. If the enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and which will act as the general base during the initial steps of the reaction?The glycine cleavage system is a group of four enzymes that together catalyze the following reaction: Use the following information to determine the sequence of reactions carried out by the glycine cleavage system:a. The first enzyme is a PLP-requiring decarboxylase.b. The second enzyme is aminomethyltransferase. This enzyme has a lipoate coenzyme.c. The third enzyme synthesizes N5,N10-methylene-THF and also forms +NH4.d. The fourth enzyme is an FAD-requiring enzyme.e. The cleavage system also requires NAD+ .One of the examples that we have used to illustrate the concept of equilibrium is the isomerization of glucose-6-phosphate (G6P) to fructose-6-phosphate (F6P), which is the second step in g ycolysis. Draw a graph to show how the reaction Gibbs energy varies with the fraction fof F6P in solution.Label the regions of the graph that correspond to the formation of F6P and G6P being spontaneous, respectively.
- Name the following enzymes:a. enzyme responsible for the cutting of the sugar on the nonreducing ends of glycogen branches b. enzyme that is only present in the liver and kidney during glycogen utilization c. enzyme that catalyzes the transfer of a two-carbon fragment from a ketose donor to an aldose acceptor in PPPThe highest energy point of the serine protease reaction is the formation of the tetrahedral oxyanion intermediate on the original carbonyl carbon of the scissile peptide bond. True or False? DIPF is an irreversible inhibitor of serine proteases. True or False? The acyl-enzyme intermediate is the transition state of the reaction. True or False? Serine proteases are classified as isomerases. True or False?a-Keto acids other than a-ketoglutarate can accept the amino group from pyridoxamine in enzyme-catalyzed transamination reactions. What amino acids are formed when the following a-keto acids accept the amino group?O OO O Opyruvate oxaloacetate
- When glucose is reduced, only one alditol is produced.When fructose undergoes the same reaction, however,two diasteriomeric sugars are produced. Draw theirstructures.In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.The cleavage of fructose-1,6-bisphosphate to glyceraldehyde3-phosphate and dihydroxyacetone phosphate is an exampleof an __________________ reaction