Question

It was found that a reveryble inhibitor and a substate bind an encyme, but ac different sites. The inhibitor was quite potent at reducing ensyme activity, but a Scatchard analysis indicated it could not achually bind the ensyme unless the substract was bound first. These resuls led to what conclusion? It was a competiture intilition. It was a moed inhibitor. It was all uncompetive inhibitor. It mas an allosteric eodulator. Reas a medinismbaned inactivator.

Name: it was found that a reveryble inhibitor and a substate bind an encyme but ac different sites the inhibitor was quite potent at reducing ensyme activity but a scatchard analysis indicated it 18387
Uploaded: 2023-02-13T03:45:17-08:00
Duration: 3 min 59 s
Channel: Farhan Anwar
Description: it was found that a reveryble inhibitor and a substate bind an encyme but ac different sites the inhibitor was quite potent at reducing ensyme activity but a scatchard analysis indicated it 18387

          It was found that a reveryble inhibitor and a substate bind an encyme, but ac different sites. The inhibitor was quite potent at reducing ensyme activity, but a Scatchard analysis indicated it could not achually bind the ensyme unless the substract was bound first. These resuls led to what conclusion?
It was a competiture intilition.
It was a moed inhibitor.
It was all uncompetive inhibitor.
It mas an allosteric eodulator.
Reas a medinismbaned inactivator.

it was found that a reveryble inhibitor and a substate bind an encyme but ac different sites the inhibitor was quite potent at reducing ensyme activity but a scatchard analysis indicated it 18387

Added by Jennifer B.

Biology for AP Courses

Julianne Zedalis, John Eggebrecht

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Solved by Expert Farhan Anwar

02/13/2023

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The inhibitor was quite potent at reducing enzyme activity, but a Scatchard analysis indicated it could not actually bind the enzyme unless the substrate was bound first. These results led to what conclusion? (A) It was a competitive inhibitor. (B) It was a mixed Show more…

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It was found that a reveryble inhibitor and a substate bind an encyme, but ac different sites. The inhibitor was quite potent at reducing ensyme activity, but a Scatchard analysis indicated it could not achually bind the ensyme unless the substract was bound first. These resuls led to what conclusion? It was a competiture intilition. It was a moed inhibitor. It was all uncompetive inhibitor. It mas an allosteric eodulator. Reas a medinismbaned inactivator.