This phenomenon is known as substrate inhibition and the mathematical description of it requires an inhibition constant (Ki) as well as the usual kinetic parameters (Km and Vmax). Fitting the 3-parameter substrate inhibition expression to data that might reasonably be described by the 2-parameter ...
A. Vmax增加,Km增加 B. Vmax 减小,Km减小 C. Vmax不变,Km增加 D. Vmax不变,Km减小 查看完整题目与答案 是“两个一百年”奋斗目标的第一个百年奋斗目标,是我们党向人民、向历史作出的庄严承诺。 (),是“两个一百年”奋斗目标的第一个百年奋斗目标,是我们党向人民、向历史作出的庄严承诺...
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What value of(s), as a fraction of km, is required to obtain 20% vmax?(s)equals: Michaelis-Menten Kinetics: Michaelis-Menten kinetics describe enzyme activity under specific conditions. The concentration of the enzyme is held constant while the concentration of the substrate...
What is the distance(in meters)between adject peaks(antinodes)in your standing wave plot? Use the distance you found above to calculate the wavelength(in meters).Note that the wavelength is twice the distance between adjacent peaks. So take...
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A lower Vmax means that the enzyme is operating in sub-optimal conditions. This may be because physical conditions such as temperature and pH are not...Become a member and unlock all Study Answers Start today. Try it now Create an account Ask a question Our experts can answer your ...
Kinetic analysis of the residual enzyme activity from our most conservative construct, Arg211---, determined an apparent Vmax approximately 400-fold reduced from that of the wild type enzyme but detected no change in the apparent Km. Additionally, the pH optimum of this mutant enzyme was narrower...
At this time, the enzyme maximum vitality reaches 29.1 U/mg; and 4 ~ 50 ℃ , hot treatment β- glucosidase BGL22384 H < /span> Later, the enzyme vitality of 70% above , The thermal stability is better its dynamics parameters vmax is 576 μmol/(l · min), km is 0.296 mmol/L ....