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 isshown 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 structuresof ceruloplasmin.

Ceruloplasmin is a copper containing globulin which helps in the transport of copper in the…

Answered: Ceruloplasmin is a blue-colored…

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) illustrate in molecular detail how hemoglobin's reduced oxygen affinity is caused by protonation of the histidine side chain. b) what is the pKa of the histidine side-chain ionizable group expected to have?|
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*
What term best describes the isomeric relationship between alpha-D- glucopyranose and alpha-L-glucopyranose? A) structural isomers B) enantiomers C) epimers D) diastereoisomers, but not epimers E) not isomers
Which of the following statements regarding the nitrogenous base guanine is FALSE? A) ALL of these statements are TRUE B) the enol form of guanine base-pairs with thymine C) guanine undergoes a tautomeric shift between a keto and an enol form D) the keto form of guanine base-pairs with cytosine E) an alcohol (-OH) group is present in guanine's enol form, but absent in the keto form F) guanine’s keto form is more stable than its enol form
Indicate the FALSE alternative: a) The formation of osazones is a characteristic reaction of aldoses and ketoses. b) Disaccharides formed by aldoses with 1-1' linkages do not have reducing power or mutarotation. c) Glycosides have no reducing power. d) Glycosidic bonds allow the formation of branched structures. e) A characteristic of alditols is that they all have optical activity.
there are A-D questions to this picture set up. A) What enzyme catalyzes this reaction? B) What is Delta G, please answer in Joules, K=19 C) If concentration of Glucose-1_Phosphate is 48.82 uM at equalibrium, what is the concentration of Glucose-6-phosphate in uM? D) If the reaction is NOT at equalibrium, what is delta G at 25C if the concentration of Glucose-1-phosphate is 15.04 uM and concentration of Glucose -6-phosphate is 1.62 mM? please answer in Joules and in significant figures. *note, 10^3uM in 1 mM Thank you!!
Glucose-6- phosphatase catalyzes the following reaction: glucose – 6-phosphate + H2O = glucose + phosphate. Glucose-6- phosphatase would be classified as a(n) a) kinase b) hydrolase c) lyase d) oxidoreductase If ∆G for a biochemical reaction has a positive value, this means: a) the reaction will proceed very rapidly b) the reaction will proceed very slowly c) the reaction will generate heat d) The reaction requires energy input to proceed. Which thermodynamic parameter do enzymes change? A) entropy b) activation energy c) enthalpy d) all of these Enzymes have which effect on the chemical equilibrium of a biochemical reaction? A) the equilibrium shifts to favor products b) the equilibrium shifts to favor reactants c) The equilibrium does not shift, but gets there faster d) a new equilibrium is formed
From the three figures below, indicate which represents best the catalytic pocket of trypsin, a serine protease, secreted by acinar pancreatic cells. C) A) A. Figure A. B.Figure B. ⒸC. Figure C. Asp 189 B) Asp 189 Val 190 Val 216 work of Val 216 Val 190
Cottage cheese and many other cheeses are produced by adding the enzyme rennin to milk, producing curds and whey. a) Design an experiment to determine the pH at which rennin is most effective. How will you measure the results? b) What are tests that can be used to detect protein, sugars, and fats? How can these tests to determine the chemical makeup of curds and whey?
a) At what pH will you try to bind lysozyme to a cation exchanger? b) Is it possible to perform this binding even at a different pH than the one you mentioned in section a? Explain your answer. c) Is it possible to bind lysozyme to an anion exchanger as well? If so, at what pH?
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22) A) Write the structure for a generic triacvlglyceride at pH 7.4. B) Show the mechanism of a lipase including the catalytic triad and the oxyanion hole up to the tetrahedral intermediate of the cleavage of the acyl-alcohol bond. C) What is the purpose of the þxyanion hole? D) How does the catalytic triad function to lower the pKa of serine. coo coo H,N-C-H H,N-C-H CH, CH2 он Serine (S) (Ser) HN Histidine (H) (His) coo co H,N-C-H H,N-C-H H CH, Glycine (G) (Gly) coo Aspartate [D] (Asp)

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