BIOCHEMISTRY
BIOCHEMISTRY
9th Edition
ISBN: 2818440090622
Author: BERG
Publisher: MAC HIGHER
Question
Book Icon
Chapter 8, Problem 19P
Interpretation Introduction

(a)

Interpretation:

Whether the given reaction proceeds as written or not is to be stated. The final concentrations of glucose6phosphate and glucose1phosphate is to be stated.

Concept introduction:

When any reaction is at equilibrium then a constant expresses a relationship between the reactant side and the product side. This constant is known as equilibrium constant. It is denoted by Keq. The equilibrium constant is independent of the initial amount of the reactant and product.

Interpretation Introduction

(b)

Interpretation:

The cellular condition under which glucose-1-phosphate is produced at a high rate is to be stated.

Concept introduction:

When any reaction is at equilibrium then a constant expresses a relationship between the reactant side and the product side. This constant is known as equilibrium constant. It is denoted by Keq. The equilibrium constant is independent of the initial amount of the reactant and product.

Blurred answer
Students have asked these similar questions
Please balance the reaction below. Considering the pe0 of Pb2+/Pb0 and O2/H2O are -2.13 and 14.5, respectively, will the oxidation of Pb0 by oxygen occur under conditions: pH 8, [Pb2+] = 5x10-8 M, [O2(aq)] = 2.5x10-4 M? Pb0 + O2 + H+ → Pb2+ + H2O
At 300 K, what fold improvement in a reaction rate do you expect if AG* is brought down from 40 kJ/mol to 20 kJ/mol, without changing of the reaction mechanism, as a result of enzymatic catalysis? е. f. there will be (1) no effect, (2) an increase, or (3) a decrease? The following may or may not be affected by the addition of an enzyme to a chemical reaction. State if A) activation energy of the reaction B) standard free energy of the reaction C) time to reach equilibrium D) equilibrium constant of the reaction E) initial velocity of the reaction g. Remember the simple kinetic mechanism for an enzyme-catalyzed reaction. It was reported that the rate-limiting step is the following reaction k2 ES > P Under these circumstances, the Michaelis constant becomes equivalent to A) [S], when Vo = Vmax B) Turnover number C) Specificity constant D) kcat E) the dissociation constant for the Enzyme-Substrate (ES) complex
6-25 substrate-band enzyme concentrations. The the turnover number is equal to umax- b) V=Umax •57(Km+S) anstont For an enzyme that displays Michaelis-Menten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? a) [S] = KM C) d) e) [S] = 0.5KM [S] = = 0.1KM [S] = 2KM [S] = 10KM w reactores -maximumrate of reaction boteles conc. Would you expect the structure of a competitive inhibitor of a given enzyme to be similar to that of its substrate?
Knowledge Booster
Background pattern image
Similar questions
SEE MORE QUESTIONS
Recommended textbooks for you
  • Text book image
    Biochemistry
    Biochemistry
    ISBN:9781305577206
    Author:Reginald H. Garrett, Charles M. Grisham
    Publisher:Cengage Learning
    Text book image
    Biochemistry
    Biochemistry
    ISBN:9781305961135
    Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
    Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning