9th Edition

ISBN: 9781305961135

Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher: Cengage Learning

Concept explainers

We generally tend to think of proteins only from a dietary lens, as a component of what we eat. However, they are among the most important and abundant organic macromolecules in the human body, with diverse structures and functions. Every cell contains t…

Protein Expression

The method by which living organisms synthesize proteins and further modify and regulate them is called protein expression. Protein expression plays a significant role in several types of research and is highly utilized in molecular biology, biochemistry…

Videos

Textbook Question

Chapter 6, Problem 26RE

MATHEMATICAL Determine the values of K M and V max for the decarboxylation of a β -keto acid given the following data.

substrate concentration ( molL − 1 ) Velocity ( m M min − 1 ) 2.500 1.000 0.714 0.526 0.250 0.588 0.500 0.417 0.370 0.256

Expert Solution & Answer

Trending nowThis is a popular solution!

See solution

Check out sample textbook solution

Chapter 6, Problem 25RE

Chapter 6, Problem 27RE

Students have asked these similar questions

61. MATHEMATICAL For the following aspartase reaction (see Ques- tion 28) in the presence of the inhibitor hydroxymethylaspar- tate, determine K and whether the inhibition is competitive or noncompetitive. [S] (molarity) V, No Inhibitor (arbitrary units) V, Inhibitor Present (same arbitrary units) :21×10¹01 0.026 TOIV 0.0109 9 5 X 10 0.092 0.040 0.086 0.120 10-3 IPO? 2.5 10-³ 5×10 211 0.150 09M ein 5 X 10-3 0.165 20 mys 0.142

ENZYME KINETICS ANALYSIS of 6 Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess causes gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student researcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO which uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the Lineweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table 2 and paste a copy of your Lineweaver-Burk plot. submit the picture of your output in PNG or JPG format. Table 1. Enzyme Kinetic Data Velocity, mM/s [S], mM Хan Kmp Cha 0.492 0.0678 0.0351 0.0615 0.211 0.0531 0.0261 0.0451 0.087 0.0298 0.0157 0.0211 0.048 0.0195 0.0091 0.0142 0.029 0.0127 0.0067 0.0081 Table 2. Enzyme Kinetic Parameters Xanthine Kaempferol Chlorogenic acid Parameters Vmax Км Type of Inhibition Mode of Binding NA NA Lineweaver-Burk Plot

Initial rate data for an enzyme that obeys Michaelis–Menten kinetics areshown in the following table. When the enzyme concentration is 3 nmolml-1, a Lineweaver–Burk plot of this data gives a line with a y-intercept of0.00426 (μmol-1 ml s). (a) Calculate kcat for the reaction.(b) Calculate KM for the enzyme.(c) When the reactions in part (b) are repeated in the presence of 12 μM ofan uncompetitive inhibitor, the y-intercept of the Lineweaver–Burk plotis 0.352 (μmol-1 ml s). Calculate K′I for this inhibitor.

Chapter 6 Solutions

Biochemistry

Ch. 6 - RECALL How does the catalytic effectiveness of...Ch. 6 - RECALL Are all enzymes proteins?Ch. 6 - MATHEMATICAL Catalase breaks down hydrogen...Ch. 6 - REFLECT AND APPLY Give two reasons why enzyme...Ch. 6 - RECALL For the reaction of glucose with oxygen to...Ch. 6 - REFLECT AND APPLY Would nature rely on the same...Ch. 6 - REFLECT AND APPLY Suggest a reason why heating a...Ch. 6 - REFLECT AND APPLY A model is proposed to explain...Ch. 6 - REFLECT AND APPLY Does the presence of a catalyst...Ch. 6 - REFLECT AND APPLY What effect does a catalyst have...

Knowledge Booster

Learn more about

Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.