Questions tagged [enzyme-kinetics]

Enzyme kinetics is the study of the rates of enzyme-catalysed reactions

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4
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2answers
3k views

Identifying type of inhibitor from $K_m$ and $V_{max}$

Apparently it is possible to identify whether an inhibitor is competitive or non-competitive from graphs of substrate concentration (x axis) and rate of reaction (y axis). There needs to be a line ...
9
votes
1answer
2k views

Understanding Enzyme saturation curve

From the above picture it can be seen that, in the region "B" the activity of enzyme is not proportional to the substrate concentration. Why don't we achieve enzyme saturation linearly? Why do we go ...
4
votes
2answers
459 views

Enzyme kinetics at the chemical level

I am stumped by two questions: Why do we take only the initial 10%(or may be 9.99999....%) of S conversion as the rate of the enzyme reaction. why not more than 10%? Why doesn't the velocity keep on ...
6
votes
2answers
2k views

Why are enzyme-catalysed reactions slower at lower substrate concentration?

Suppose I'm using 200 nmoles of enzyme and 2 mmoles of substrate. The enzyme should be saturated but if I use 50 mmoles of substrate, the reaction will be faster. Why? I just can't get it! Even at ...
1
vote
1answer
257 views

Enzyme kinetics: recommended literature to grasp the concepts better

I have had a few biochemistry courses, but I still feel confused and a bit scared each time they try to explain and apply enzyme kinetics or even chemometrics in different situation during class. On ...
5
votes
1answer
6k views

Does pH affect Michaelis constant?

I have been trying to confirm the Km of a substrate (which is 34 +/- 4 mM). This value was obtained in 50 mM MOPS, pH 6.3. I conducted my kinetics assay in a buffer of pH 7 and obtained a Km value in ...
2
votes
2answers
2k views

Why would an Eadie-Hofstee Plot be non-linear? [closed]

Besides cooperativity between multiple active sites on an enzyme, what are the other reasons for the Eadie-Hofstee plot to be non-linear?
1
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2answers
183 views

How can ionized amino acid form be important for the catalytic activity?

I can imagine that protonated amino acid form, particularly at the active site, is important for the catalytic activity so hydrogen bonds can be created between the substrate and the enzyme. However, ...