When HBC is added to a buffer solition on enoyl coA hydratase in D218O it was fo

Question

When HBC is added to a buffer solition on enoyl coA hydratase in D218O it was found that the enzyme catalyzes the exchange of deuterium between the solvent and the hydroxyl oxygen of HBC and the exchange of deuterium between thhe solvent and a carbon bound hydrogen in HBC. However, the rate of feuterium exchange was four times to be faster than the rate of 18O exchange. When 18O-HBC was used as a substrate it was found that kcat/km was reduced about 5%.

So outline a mechanism for this reaction indicating the rate limiting step, that is consistent with the datat as well as explain why your mechanism is resonable.

Explanation / Answer

WHEN THERE ARE THE NUMBER OF SUBSTRATE FOR THE ENZYME i.e,    mutisubstrate reaction the rate of K cat and K m constantly decreases , because of the mutiple sites for the substrate for the enzyme . in general the hydrolases add water to across the hydrogen bond . the K cat indicates the rate of formation of product , so it indicates the rate of the reaction km indicates the affinity of the enzyme for the substrate the lower km indicates the low affinity and vice vers , hence large km indicates the low K cat values . in the above reaction there is a reduction in the k cat and k m values indicating the above enzyme has a two subtrates for binding , and it is Bi substrate reaction. the above example is the exchange of the water or hydrogen atoms across the HBc memberane by using the enzyme enoynl hydrolases as they add water across the double bond , deteruim oxide exchanges the hydrogen atoms with the help of water hydogen atoms . the rate of reaction is is extracellular , so the above reaction is reasonnablyy be a rate limiting step

Related Questions

Navigate

• Browse (All)
• Browse W
• Subjects

Integrity-first tutoring: explanations and feedback only — we do not complete graded work. Learn more.