DOC PREVIEW
TAMU BICH 410 - 10_-_Enzyme_kinetics-2

This preview shows page 1-2-3-4-28-29-30-31-58-59-60-61 out of 61 pages.

Save
View full document
Premium Document
Do you want full access? Go Premium and unlock all 61 pages.
Access to all documents
Download any document
Ad free experience

Unformatted text preview:

1 2 3 Enzyme kinetics provides an avenue to explore how enzymes achieve the reduction in activation energy and other effects involved in catalysis 4 5 6 Study carefully how the levels of all the substrates products and enzyme complexes change with time In succeeding images we will make simplifying assumptions that allow us to use enzyme kinetics more effectively 7 8 9 10 The first crucial simplification is to use curve tangent fitting to estimate the initial velocity of the reaction This allows us to ignore changes in substrate and product concentrations as the reaction proceeds 11 In general the formation of steady state levels of the enzyme substrate complex ES and free enzyme E can be assumed to be so rapid as to be effectively instantaneous Michaelis Menten kinetics assumes this state assuming the status diagramed in the assay zone above 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60


View Full Document

TAMU BICH 410 - 10_-_Enzyme_kinetics-2

Download 10_-_Enzyme_kinetics-2
Our administrator received your request to download this document. We will send you the file to your email shortly.
Loading Unlocking...
Login

Join to view 10_-_Enzyme_kinetics-2 and access 3M+ class-specific study document.

or
We will never post anything without your permission.
Don't have an account?
Sign Up

Join to view 10_-_Enzyme_kinetics-2 and access 3M+ class-specific study document.

or

By creating an account you agree to our Privacy Policy and Terms Of Use

Already a member?