What is a glycosyltransferase? Choose all that apply Group of answer choices Catalyzes the formation of a bond between a sugar and an amino acid An enzyme that cleaves a glycosidic bond An enzyme that catalyzes the formation of a glycosidic bond An enzyme that transfers nucleotide-sugars from the cytoplasm

What is a glycosyltransferase? Choose all that apply Group of answer choices Catalyzes the formation of a bond between a sugar and an amino acid An enzyme that cleaves a glycosidic bond An enzyme that catalyzes the formation of a glycosidic bond An enzyme that transfers nucleotide-sugars from the cytoplasm

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 7TYK: In an enzymatic reaction: a. the enzyme leaves the reaction chemically unchanged. b. if the enzyme...

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10. Chymotrypsin is a serine protease enzyme. The Km for the reaction of chymotrypsin with N-acetylvaline ethyl ester is 8.8*102, and the Km for the reaction of chymotrypsin with N- acetyltyrosine ethyl ester is 6.6*10“ M. catalytic triad Ser 195 His 57 Gly 193 N-H OH R-N- Ca N-H O-C- Asp 102 N-acetyl valine N-acetyl tyrosine Chymotrypsin Active Site a. What is the nucleophile here and how is it activated? b. Which substrate has an apparent higher affinity for the enzyme. c. Propose a reason for the difference in affinity based on the shape of each of the substrates (see active site figure, cleaves on the C-side of aromatic residues).
5. Shown below are the first steps in the mechanism of a cysteine protease, which catalyses amide bond hydrolysis in a similar manner as serine proteases. (a) Complete this mechanisms, and (b) sketch the approximate reaction coordinate diagram for this catalyzed reaction relative to the uncatalyzed proteolysis. HN N HN cysteine protease
Protease enzymes cleave proteins by hydrolyzing peptide bonds. The strategy for each type of metalloprotease begins with generating a nucleophile that attacks the peptide bond that attacks the peptide carbonyl group. O Macmillan Learning On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a metalloprotease. Metalloproteases H R₁ HN Zn Enz 2+ R₂ Draw curved arrows on the pre-drawn structures to show the metalloprotease mechanism. If you need to reset the structures, click More followed by Reset Drawing. Select Draw Templates Groups More B - H Enz H H с R1 | : HN O | Zn 2+ B R2 N Zn Erase
2. Phospholipases (PL) are enzymes that hydrolyzes PLA1 phospholipids into fatty acids and other lipophilic substances. Different class of phospholipase cleaves different bond in a phospholipid molecule. Shown on the right are the cleavage sites of four classes of PL: PLA1, PLA2, PLC, and PLD. R1 R2 -O-P-'·O-R3 (a) Write down the reaction of phosphatidylcholine (PC) cleaved by PLA2. Suppose the two acyl groups are R1 and R2 as shown in the figure. Make sure the chiral carbons in the reactions have the right stereochemistry (i.e., use wedge-dash notation), and the charges on the atoms reflect the molecule in neutral pH. PLA2 PLC PLD (b) Which PL is needed in order to release choline for salvage? (c) What is the structure and name of the remaining molecule after cleaving PC by the PL in (b) and releasing choline. No need to use wedge-dash notation. (d) The molecule in (c) can be used to synthesize triacylglycerol. Write down the reactions, including the enzymes and cofactors. Assume the…
Which of the following statements about the allosteric site is true? a. The allosteric site is a second active site on a substrate in a metabolic pathway. b. The allosteric site on an enzyme can allow the product of a metabolic pathway to inhibit that enzyme and stop the pathway. c. When the allosteric site of an enzyme is occupied, the reaction is irreversible and the enzyme cannot react again. d. An allosteric activator prevents binding at the active site. e. An enzyme that possesses allosteric sites does not possess an active site.
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.
1. Draw the structure of triglyceride containing the fatty acids palmitic, oleic, and linoleic. How many Hydrogen atoms are needed in the its catalytic hydrogenation? 2. Draw the structure of Phosphatidylserine that contains oleic and arachidonic acid. What role does it play in the cell?
5. protein = D-Glucosaminate-6-phosphate Ammonia-lyase Based on the structural properties of your protein above , how resistant (or sensitive) would your protein be to heat denaturation and why?
I'm very confused about these diagrams. Can anyone tell me how to understand them? Or where to look to find the answers?
5. Consider the reaction for assembly of a tetrapeptide from for amino acids: Serine + Proline + Alanine + Methionine ----> SPAM tetrapeptide Is this reaction anabolic or catabolic? Is this a positive or negative delta G reaction? List at least three other terms you could use to describe this reaction. 6. Consider the reaction: Glutamic acid + Ammonia + ATP ----> Glutamate + ADP + Pi Is this reaction anabolic or catabolic? Is this a positive or negative delta G reaction? This is actually an example of a coupled reaction! Briefly, explain why reaction coupling is required, and how it works in this example.