Concerning enzymatic activity, a larger Km value indicates a/an:Select one:O lower affinity for its substrateO inhibitory processO larger enzymeO larger VmaxO greater affinity for the substrateWhich is the least common type of chemical bond?Select one:O HydrogenO PeptideO CovalentO lonicO DisulphideD-gluconic acid is:Select one:O an integral membrane proteinO a codonO an oxidized sugarO phosphorylatedO a large lipid molecule

Enzymes are biological catalysts that increase the rate of the reaction they catalyze with respect…

Answered: Concerning enzymatic activity, a larger…

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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From the following data of an enzymatic reaction, determine the type of inhibition, the KM for the substrate and Ki for the enzyme-inhibitor complex. [S] mM 2.0 3.0 4.0 10.0 15.0 [P] mM/h (without inhibitor) 139 179 213 313 370 [P] mM/h ([I]=6mM) 88 121 149 257 313
Which of the following statements is true O Sphingomyelin posses phosphoryl serine in addition to two long hydrocarbon chains, one contributed by a fatty acid and the other by sphingosine OLipid compositions of membrane mono-layers are symmetrical O Unsaturated fatty acids have double bond(s) in the cis configuration In ABO blood typing, lack of glycosyltransferase and galactosyltransferase produces AB blood group
Some enzymes can be regulated by covalent modification, in which a group is covalently bonded to an amino acid side chain. Phosphorylation of side chains is a common regulatory covalent modification. In this essay, you will explore phosphorylation of side chains. Compare and contrast the types of interactions a free alcohol side chain such as serine could make with that of a phosphorylated alcohol such as phosphoserine (pSer). Could this modification affect the 3D structure of the protein? How? Imagine you are trying to separate a protein containing an unphosphorylated S residue from the same protein containing a pSer residue. Discuss how you could use ion-exchange chromatography to separate these two proteins
Which class of enzymes have sigmoid or S-shaped plots of the rate of a reaction, v, versus the substrate concentration, [S], instead of the hyperbolic curves of the Michaelis-Menten equation? transferases holoenzymes O hydrolases O allosteric enzymes O ribozymes
3.18: An enzyme E binds a substrate S and a cofactor C. The equilibrium dissociation constantKd,S of the enzyme-substrate complex ES is 1 μM, for EC it is 10 μM. When the cofactor Cis present, K’d,S is decreased to 0.1 μM. What is the value for the dissociation constant K’d,C of the enzyme-cofactor complex in the presence of substrate S? Calculate the interactionenergy ΔΔGint for cofactor and substrate binding.
The process of protein decomposition by pepsin enzymes in stomach is assumed and modeled as a batch reactor. If the protein concentration over time is measured as follows: Write the relationship between time (t), protein concentration (CA). Assuming that the enzyme reaction follows Michaelis-Menten kinetics, write the required constant (Vmax, Km), and the initial concentration of the protein is CA0.
Which of the following are true when enzymes and substrate interact? kı E + S ● ES- -P k-1 the rate of the formation of ES = k1 [ES] the rate of the formation of the product = k2[ES] k1 [ES] = k-1 [ES] the rate of breakdown of ES to reform the enzyme and substrate = K-1[E][S] the rate of formation of ES = k1[E][S]
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB O a. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O b. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction O c. The enzyme stabilizes the transition state for the reaction Od. The reaction is exergonic е. The reaction is now spontaneous due to the addition of enzyme Released Energy
1. A ligand binds more tightly to the folded state (N) of a protein than to the unfolded state (U). Show that the ligand stabilizes the protein and calculate by how much (DDGfold = ?) 2. An enzyme E binds a substrate S and a cofactor C. The equilibrium dissociation constant Kd,S of the enzyme-substrate complex ES is 1 μM, for EC it is 10 μM. When the cofactor C is present, Kd,s’ is decreased to 0.1 μM. What is the value for the dissociation constant Kd,C’ of the enzyme-cofactor complexing the presence of substrate S? Calculate the interaction energy DDGint for cofactor and substrate binding.
I have a fill in the blank question. "1) Heterophobic or Homotrophic effects= are changes in affinity due to substrate binding and cooperativity between different subunits. They give Allosteric rate curves their Sigmoid shape. 2) Hetero or Homotrophic effects=are changes in affinity due to binding of an effector to an Allosteric site. Allosteric sites are usually 3)located outside or inside the active site. Positive Allosteric effectors (activators) shift the rate curve 4) Left or Right, where Negative effectors shift it 5) right or left. Positive Allosteric effectors usually stabalize the 6)T or R state. Negative efftors usually satbalize the R state." Thank You!!!
Although we have introduced catalytic strategies separately, an enzyme typically employs more than one during a reaction. The catalytic strategies employed by serine protease include: Select one or more: O a. reduction of ASt b. transition state stabilization Oc. metal-assisted catalysis O d. acid/base catalysis O e. covalent catalysis

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