题目
题目

BIOL3611.13541.202610 InClassQuiz_Enzyme Kinetics

单项选择题

When k–1 > k2 (that is, when the rate constant for dissociation of the enzyme substrate complex is greater than the rate constant for conversion to product), the KM is most analogous to  

选项
A.the Kd or dissociation constant
B.the Ka.
C.the kcat.
D.1/kcat.
查看解析

查看解析

标准答案
Please login to view
思路分析
Let's walk through each option carefully and connect them to the given condition k-1 > k2. Option 1: the Kd or dissociation constant. When the rate of dissociation of the enzyme–substrate complex (k-1) is greater than the rate of conversion to product (k2), the Michaelis......Login to view full explanation

登录即可查看完整答案

我们收录了全球超50000道考试原题与详细解析,现在登录,立即获得答案。

类似问题

Since citrate synthase exhibits sequential, ordered kinetics:

Indicate below the interpretation for the graph above

When Chapman et al. (1999) were determining the 5MDH structure of malate dehydrogenase, they provided the enzyme with tetrahydroNAD Links to an external site. instead of the closely-related endogenous substrate NAD+ Links to an external site. . They also provided alpha-ketomalonate Links to an external site. instead of the endogenous substrate malate Links to an external site. .    The authors said that they had to use this approach because "stable ternary complexes suitable for crystallographic analysis are hard to devise" and that either one or both of the substrates would need to be an analog.   This enzyme typically oxidizes a 4-carbon skeleton (malate), and they looked for suitable analogs. They noted that "alpha-ketomalonate is chemically stable, binds with reasonable affinity (Km = 1.0 mM) and is efficiently reduced... (kcat = 300 s -1)."   What would 'poor' Km and kcat values have looked like in a 'highly disappointing' candidate? Think back to previous lab coverage on this topic (3A, 4A). What were they looking for when making these comparisons? Which direction is 'impressive' for each of these two enzyme descriptors?   To avoid a disappointing result they wanted to make sure that the alpha-ketomalonate Km was fairly ______ and the kcat was fairly ______ in order to reasonably mimic a natural substrate like malate.  

What would be the result of an enzyme having a greater binding energy for the substrate than for the transition state?

更多留学生实用工具

加入我们,立即解锁 海量真题独家解析,让复习快人一步!