Identify the enzyme that carry out the below reaction and denotes the nature of the enzyme? UDP-galactose + N-acetylglucosamine ~ UDP + N-acetyllactosamine
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Identify the enzyme that carry out the below reaction and denotes the nature of the enzyme?
UDP-galactose + N-acetylglucosamine ~ UDP + N-acetyllactosamine
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- UDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?Explain the basis for the following statement. For efficient conver- sion of galactose to glucose-1-phosphate, UDP-glucose need be present in catalytic amounts only.Given the following reaction, identify the class and subclass of the enzyme involved. H. CH2OH H-C-OH C=0 но-с-н но-с-н H-C-OH H-C-OH H-C-OH H-C-OH CH2OPO,2 CH2OPO,2- Class: [ Select] [ Select ] Ligase Hydrolase Lyase Subcla Transferase Isomerase Oxidoreductase
- If glucokinase has a higher Km for glucose than does hexokinase, but can only bind to D-glucose, while hexokinase can bind to several hexose sugars (like D-glucose, D-mannose, and D-fructose), then: glucokinase has both a higher affinity and a higher specificity for D-glucose than does hexokinase glucokinase has both a lower affinity and a lower specificity for D-glucose than does hexokinase glucokinase has a higher affinity but a lower specificity for D-glucose than does hexokinase glucokinase has a lower affinity but a higher specificity for D-glucose than does hexokinase all of the aboveIndicate the general type of enzyme that mediates each glycolysis reaction depicted below. (e.g. Transferase, Oxidoreductase, Kinase, Hydrolase, Lyase, or Isomerase) iii. O H Glyceraldehyde-3-phosphate → 1,3-Bisphosphoglycerate H-C-OH + NAD CH₂O-P + P₁ H-O- -C-H Glucose →→ Glucose-6-phosphate H b 0 OH HO OH H-C- 0 -H HO- H ОН H-C-OH + NADH +H+ CH₂O P P ATP ADP 1 H (P-O- -C- H H HO OH 2-Phosphoglycerate → Phosphoenolpyruvate 0 OH H ОН -O~(P) + HOHA carboxypeptidase is a metalloenyme (its active site contains one or more metal ions essential for the function) that catalyzes the hydrolysis of the peptide bond of the terminal amino acid of a polypeptide chain (where the free carboxyl group occurs). The binding of an L-alanyl-L-tyrosine peptide substrate in the active site of the enzyme is represented in the scheme below: Glu Zn++ COO™ OH H3C CH₂ HC NH IO C H H Poche apolaire -H H O+N: C N H H H NH₂ Arg 145 Туг 248 NB: This scheme gives a planar representation of the spatial structure of the active site where indicated contacts (hatched lines) are supposed to occur in the 3D structure of the enzyme. 1- Describe the interactions that occur between the ligand and amino acid residues of the active site. 2- What would be the impact on the Km value if we replace L-alanyl-L-tyrosine by the following substrates: L-alanyl-L-phenylalanine; L-alanyl-L-aspartate; L-aspartyl-L- tyrosine.
- Which reaction is irreversible? oxidized glutathione + NADPH + H+ → reduced glutathione + NADP+ ribulose 5-phosphate → ribose 5-phosphate glucose 6-phosphate + NADP+ → 6-phosphoglucono-δ-lactone + NADPH + H+ sedoheptulose 7-phosphate + glyceraldehyde 6-phosphate → fructose 6-phosphate + erythrose 4-phosphate ribulose 5-phosphate → xylulose 5-phosphatethe following is a coenzyme or cofactor involved in enzymatic reaction. identify the biochemical role that S-adenosylmethionine plays within a biochemical tranformation.The enzyme ATCase (Aspartate TransCarbamoylase) catalyzes an early step in the synthesis of the pyrimidine nucleotides. The activities of the ATCase reactions are shown in the following plots. Which one of the following statements is most correct description about this enzyme and/or this enzyme-catalyzed reaction? ATP No allosteric effectors Vo CTP ATCase 10 20 30 40 (Aspartate] (mM) O A. This enzyme is allosterically inhibited by ATP. B. This enzyme is composed of multiple subunits. C. "ATP" binds to catalytic subunits of ATCase. O D."CTP" binds to the R-state enzyme. O E. At high concentrations of ATP, ATP binds to the T-state enzyme, thus increase the affinity for the substrate [S].
- Myristoleic acid is a monounsaturated fatty acid found in small amounts in a variety of foods. Calculate the net ATP yield from the complete β-oxidation of myristoleic acid. The formula of myristoleic acid is shown below (it is assumed that the total ATP production is the same for both saturated and unsaturated fatty acids having the same carbon chain length). CH3-(CH2)3-CHCH-(CH2)7-COOH (Given: The oxidation of one NADH yields 2.5 ATP; the oxidation of one FADH2 yields 1.5 ATP; and the oxidation of one acetyl CoA yields 10 ATP. ) Group of answer choices a. 96 ATP b. 92 ATP c. 94 ATP d. 34 ATP e. 36 ATPChoose the CORRECT sequence of glycine formation. transamination of 3-phosphoglycerate → hydrolysis of 3-phosphohydroxypyruvate → hydrolysis of 3-phosphoserine → transfer of the side-chain methylene group of cysteine to tetrahydrofolate → glycine transamination of 3-phosphohydroxypyruvate → oxidation of 3-phosphoglycerate → transfer of the side-chain amino group of serine to tetrahydrofolate → glycine oxidation of 3-phosphoglycerate → oxidation of 3-phosphohydroxypyruvate → hydrolysis of 3-phosphoserine → glycine transamination of 3-phosphohydroxypyruvate → hydrolysis of 3-phosphoserine → oxidation of 3-phosphoglycerate →transfer of the side-chain methylene group of serine to tetrahydrofolate → glycine oxidation of 3-phosphoglycerate → transamination of 3-phosphohydroxypyruvate → hydrolysis of 3-phosphoserine → transfer of the side-chain methylene group of serine to tetrahydrofolate → glycineFor the following reactions, name both the enzyme that catalyzes the reaction and the required coenzyme: