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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A point mutation in Hb diminishes hydrophobicity at the heme. Which of the following impacts would you predict? . Increased oxidation of Fe2+ and loss of O2 binding b. Decreased negative charges needed at the dimer/dimer interface to stabilize the T-state c. Decreased positive charges needed at the dimer/dimer interface to stabilize the T-state d. Shift the O2 binding curve of Hb to the left e. Decreased affinity for BPG in the T-state
A mutation has occurred that results in phosphofructokinase not being able to bind ATP in its allosteric site. What impact will this mutation have on the production of ATP in the cell? Select one: a. If no ATP can bind to the allosteric site, then phosphofructokinase will not be able to add the phosphate to fructose-6-phosphate to make fructose-1,6-bisphosphate and glycolysis will not work. So no pyruvate, not cellular respiration. b. If ATP cannot bind to the allosteric site, phosphofructokinase will not be activated to make more ATP by substrate-level phosphorylation. c. No impact on the production but will not be able to effectively shut off over production of ATP with feedback inhibition.
Phosphoglycerate mutase transfers a phosphoryl group from C3 of 3-phosphoglycerate to C2 position to give 2-phosphoglycerate. Why is it important to have the phosphoryl group at position 2 rather than at C3? It was observed that the activity of some preparations of the enzyme could be increased if catalytic (very small) amount of 2, 3-bisphosphoglycerate was added to the enzyme. Give a possible explanation for this observation.
In some metalloproteins such as haemoglobin and some metalloenzymes, the Fe2+ metal is not bound to the amino acid side-chains of the protien,but to a prophrin ring called a heme prosthetic group. How does the heme coordinate to the iron?
The glycosaminoglycan polysaccharide chainsthat are linked to specific core proteins to form the pro-teoglycan components of the extracellular space arehighly negatively charged. How do you suppose thesenegatively charged polysaccharide chains help to estab-lish a hydrated gel-like environment around the cell? Howwould the properties of these molecules differ if the poly-saccharide chains were uncharged?
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?
The enzyme hexokinase adds a phosphate toD-glucose but ignores its mirror image, L-glucose. Supposethat you were able to synthesize hexokinase entirely fromD-amino acids, which are the mirror image of the normalL-amino acids.A. Assuming that the “D” enzyme would fold to a sta-ble conformation, what relationship would you expect it tobear to the normal “L” enzyme?B. Do you suppose the “D” enzyme would add aphosphate to L-glucose, and ignore D-glucose?
Assume that a new oxygen transport protein has been discovered in certaininvertebrate animals. X-ray diffraction of the deoxy protein reveals that ithas the dimeric structure shown in panel (a) of the accompanying figure,with a salt bridge between residues histidine 13 and aspartic acid 85. Thetwo monomers interact by salt bridges between the C- and N-termini. TheO2-binding site lies between the two iron atoms shown, which are rigidlylinked to helices A and C (see panel (b)). In the deoxy form, the spacebetween the iron atoms is too small to hold O2, and so the Fe atoms must be forced apart when O2 is bound.Answer the following questions, explaining your answer in each case interms of the structure shown below.(a) Is this molecule likely to show cooperative oxygen binding?(b) Is this molecule likely to exhibit a Bohr effect?(c) Predict the likely effect of a mutation that replaced aspartic acid 85 bya lysine residue.
Predict the locations of 14C in Aspartate synthesis using the following labeled 14C succinate. -OO14C-CH2-14CH2-14COO-
All sugar residues are in their D-isomeric forms. What kind of glycosidic linkage is between the first and second residues? What kind of glycosidic linkage is between the third and second residues?
Draw the structure of a D-glucose molecule linked to threonine via a β-glycosidic linkage.
2-carboxyarabinitol-1,5-bisphosphate (CABP) is an inhibitor of the enzyme rubisco. Among A, B, C, D, and E, which pathway would this affect most?

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