Which of the following are not one of the end products of pyrimidine catabolism? (A) NH3 (B) co2 B-alanine D Dihydroorotic acid E) Aminoisobutyrate
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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?Unbranched homopolymer of N-acetyl glucosamine is : 1.Cellulose 2.Chitin 3.Curcumin 4.Concanavalin AWhat is the end product of catabolism of the pyrimidine base thymine? What circumstances cause excess amounts of this end product, and why doesn’t this molecule (unlike uric acid, the end product of purine catabolism) cause a gout-like illness?
- Which derivative of folate is a reactant in the conversion of (a) glycine into serine? (b) homocysteine into methionine?Which of the following statements about the transamination and deamination steps of amino acid degradation is true? (A) a-ketoglutarate is always formed during a transamination between an amino acid and glutamate. (B) Transamination reactions produce glutamate that is deaminated after entering the urea cycle. (C) Free ammonia is removed from glutamate using glutamate dehydrogenase and NAD+ as an oxidizing agent. (D) The free NH4+ that is removed from glutamate during the deamination reaction is used to form glucose.(E) The carbon backbone that results from transamination enters the mitochondria to be used in the urea cycle.Ceruloplasmin is a blue-colored monomeric oxidase found in mamma- lian blood plasma. It contains multiple copper atoms per mole- cule. A ribbon representation of its three-dimensional shape is shown below: a) b) c) Identify any cofactor(s) which ceruloplasmin may possess. How do you know? Does ceruloplasmin act as an enzyme ? Describe the secondary, tertiary and quaternary structures of ceruloplasmin.
- PLP is a cofactor for a number of enzymes involved in amino acid metabolism. Give an example of reaction in which PLP participates in cleavage of the a, b, and c bonds of an amino acid, as diagrammed in shown Fig.What enzyme is catalyzed by the reaction of glutamate and NH4+ in order to yield glutamine? Is it uridylyltransferase, adenylyl transferase, glutamate transferase or glutamine synthase?Why might the compound shown below act as a transition state analog of phosphoglucose isomerase? A drawing of the normal transition state for this enzyme is needed.
- Starting from glutamine ,glycine, aspartate, N-10 formal-ThF ,how many ATP equivalents are required for purine synthesis?When the enzyme is incubated with oxaloacetate, will oxaloacetate be observed?An enzyme that catalyzes disulfide– sulfhydryl exchange reactions, called protein disulfide isomerase (PDI), has been isolated. PDI rapidly converts inactive scrambled ribonuclease into enzymatically active ribonuclease. In contrast, insulin is rapidly inactivated by PDI. What does this important observation imply about the relation between the amino acid sequence of insulin and its threedimensional structure?