Michaelis-Menten theory is valid only for a catalytic amount of enzymes and only apparent parameters can be obtained for IMERs. Others approaches could be considered (ex. frontal analysis). Why?
Do you mean DIMERS? Many enzymes only function as dimers..... they are normally treated as a single species. If you are looking for a definitive textbook on steady state enzyme kinetics then I suggest you read Segel (Enzyme Kinetics). His analyses of the various possible pathways of catalysis (and fitting the relevent equations) are still definitive. However if you are loading up your analysis with lots of active enzyme (more than catalytic) then you want to treat it as a substrate.....and this is quite a different ballgame. I'm sure there are lots of chemical kinetics papers available on this... but I'm not qualified to comment.
IMERs is "immobilized enzyme reactors". I am wondering the kinetic of immobilized enzyme will be different from the enzyme in solution? Do you have any comment on this?
Thank you for your advise, I will read Segel
The integrated form of the Michaelis-Menten equation has been used to describe immobilized enzyme reactors. See for example:
http://www1.lsbu.ac.uk/water/enztech/reactors.html
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