Folic acid is synthesized in bacteria as dihydrofolate, in a pathway startingfrom guanosine triphosphate. In this pathway, C-8 is lost as formate. Fromthe structural similarities between guanine and pterin, predict which carbonand nitrogen atoms of GTP are the precursors to N-1, C-2, C-4, N-5, C-7,N-8, and C-9 of dihydrofolate. 510PABAGIUHN 47H,N2 N1Dihydrofolate7HN8.H,N 2 N43PP.PO5'3 2ÓH ÓHGTPZI

Dihydrofolic acid is a folic acid derivative which is converted to tetrahydrofolic acid by…

Answered: Folic acid is synthesized in bacteria…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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What is the role of tyrosine in prostaglandin synthesis? Tyrosine provides the proton to the double bond initiating the cascade for ring formation. Tyrosine is the source of the hydroxyl groups that converts PGH to PGD2 and PGF. Tyrosine provides a hydrogen free radical that initiates the cascade synthesizing the prostaglandins. Tyrosine provides hydrogen bonding interaction that immobilizes arachidonic acid for conversion by cyclooxygenases (COX) Tyrosine is a catalytic residue at the active site of COX.
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?
The effect of ATP on the allosteric enzyme PFK-1 is shown below. For a given concentration of fructose 6-phosphate, the PFK-1 activity increases with increasing concentrations of ATP, but a point is reached beyond which increasing the concentration of ATP inhibits the enzyme. (a) Explain how ATP can be both a substrate and an inhibitor of PFK-1. How is the enzyme regulated by ATP? (b) In what ways is glycolysis regulated by ATP levels? (c) The inhibition of PFK-1 by ATP is diminished when the ADP concentration is high, as shown in the illustration. How can this observation be explained? *A graph is included for this question*
You have isolated a new protease that cleaves peptide bonds on the carboxyl side of Asp and Glu. Based on the enzyme's inactivation by DIPF, you suspect that it may utilize a mechanism similar to chymotrypsin. The difference in specificity might be explained by the absence of the S1 binding pocket. replacement of serine 195 with a positively charged residue. presence of a positively charged residue in the S1 binding pocket. presence of a negatively charged residue in the S1 binding pocket.
Draw the (B1-->A1) linked dissacharide formed between the C3 epimer of B-D-glucose and the C2 epimer of a-D-galactose. Explain in 1-2 sentences why (or why not) a precipiate would be observed when mixing this dissacharide in an alkaline solution of copper.
In the salvage of purines, hypoxanthine-guanine phosphoribosyltransferase (HGPRT) is responsible for which of the following processes? Conversion of hypoxanthine to xanthine Conversion of adenine to adenosine monophosphate (AMP) Conversion of guanine to guanosine monophosphate (GMP) Conversion of inosine monophosphate to inosine
I have an aqueous solution of tyrosinase but I require the solid form of tyrosinase. How would you process the aqueous solution to obtain the solid form?
Cyclic AMP (CAMP) is an important signaling molecule in cells. The synthesis and degradation of CAMP is diagrammed in the following figure: ATP ©2017 Pearson Education, Inc. 12pt Adenylyl cyclase Edit View Insert Format Tools Table Paragraph Pyrophosphate 3'c- P-P₁ 5'C BI Both caffeine (coffee, cola) and theophylline inhibit the enzyme phosphodiesterase that converts CAMP to AMP, allowing cAMP levels to temporarily remain high. Briefly discuss the possible effect of these drugs on the second messenger action of CAMP. What might the effect of caffeine of theophylline be on a signaling pathway? CAMP UA Phosphodiesterase T² H₂O AMP ⠀
the structures of chymotrypsin and other serine proteases revealed that the active sites of these enzymes shared a particular sterochemical arrangement of residues crucial to their activity. This came to be known as the catalytic triad, as it consisted of the oponyomous serine (Ser) residue, along with a histidine (His) and an aspartate (Asp) residue. Which of the following would result in the greatest decrease in function of the catalytic triad found in serine proteases? O Mutation to Ser, Cys, Asp O Mutation to Ser, His, Asp O Mutation to Cys, His, Asp O Mutation to Ser, His, Glu
The M and H subunits of lactate dehydrogenase have very similar sizes and shapes but differ in amino acidcomposition. If the only difference between the two were that theH subunit had a glutamic acid in a position where the M subunithad a serine, how would the five isozymes of LDH separate on electrophoresis using a gel at pH 8.6?
Which of the following statements are descriptions of metal ion catalysis or examples of metal ion catalysis? Choose all correct answers a Zn²+ cofactor may properly orient the substrate in the active site through ionic interactions. a covalent bond forms between enzyme and substrate lowers the energy or stabilizes the transition state or intermediate catalyst retains its original form after reaction occurs catalysts may participate in oxidation-reduction reactions by changes in the oxidation state
Glucose-1-phosphate has a higher phosphoryl group transferpotential than does glucose-6-phosphate. Review the structures of these molecules and suggest a reason for thisphenomenon.

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