enzymes Flashcards

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1
Q

How do molecules and ions increase enzyme acitivity

A

They act as cofactors and coenzymes whch bind to the active sit or allosteric site> they bind temporarily and affect charges on the site they may also interact with the substrate to increase likelihood of substrate binding to active site.

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2
Q

How do enzymes break down substrates

A

Substrate shape is complementry to enzyme so it binds to active site by induced fit and forms and enzyme substrate complex. This destabilises the bonds forming products which then leave the active site.

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3
Q

How does temperature affect enzyme action

A

Increasing tempretaure gives the molecules more kinetic energy so there are more successful collisions and more enzyme substrate complexes form. Enzymes have an optimum temperature above this hydrogen bonds that hold tertiary structure are affected so the 3d shape and active site re denatured which is irreversible.

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4
Q

Why s amylase activity low at ph4

A

As hydrogen and ionic bonds are broken as at low phs there is a high concentration of hydrogen ions which chnages the 3d or teritary tructure of the enzyme so substrate no longer fits and enzyme is denatured.

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5
Q

What is the cofactor for amylase

A

Cl-

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6
Q

What is the prosthetic group for carbonic anhydrase

A

zn2+

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7
Q

Standard deviation

A

shows the spread of data around the mean.

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8
Q

why will the initial rate be quicker

A

As more substrate is present at the start so the chance of enzyme substrate collision is increasing.

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9
Q

Why does repeating experiment improve reliability

A

as it asseses spread of results so allows a calclation of the mean

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10
Q

What is an cofactor

A

A non protein ionorganic substance that allows enzymes to carry out their actions by binding to their active site.They arent used up or changed by the reaction eg cl-

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11
Q

coenzyme

A

A non protein organic substance that allows enzymes to carry out their actions by binding to their active site.They are used and changed by the rreaction eg ATP acts as a coenzyme and is chnaged into ADP+PI

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12
Q

prosthetic groups

A

bind permanently t enzymes eg zn2+ catalyses reaction of carbonic anhydrase from co2+H2o

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13
Q

end product inhibition

A

Makes sure that a cell doesnt make too much of the final product of a metabolic pathway. final product will inhibit an enzyme from earlier on in the pathway.

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14
Q

practical reducing sugars amylae nezyme thing

A

Add the same volume of solution and heat with benedicts soluton thee should be a colour change from blue to green yellow or brick red.Then remove precipitate and ue a colorimeter. Calibrate using distilled water and use a red filter.The higher the transmission the lower the absorbance. Using known conc of maltose make a calibration curve by plotting transmission against redcing sugra conc.

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