Enzyme

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1

Enzyme

They are organic catalysts

They affect the reaction by decreasing the decreasing the activation energy.

They are proteins

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Many enzymes are conjugated protein

Proteins that consist of amino acids attached to other groups via covalent bonds) and have non protein coenzyme

Both components must be present for the enzyme to function

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substrate

The molecule upon which an enzyme acts is called the substrate

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Most enzyme catalyzed reactions are reversible

The product synthesized by an enzyme can be decomposed by the same enzyme.

An enzyme that synthesizes maltose from glucose can also hydrolyze maltose back to glucose

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Lock and key theory

More use for explaining drug interactions with receptors and enzymes

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Induced fit theory

Describes the active site as having flexibility of shape

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Best pH and temperature

Around 40

7.2 pH

Pepsin works in 2 pH

Pancreatic enzymes work in 8.5 pH

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Competitive inhibition

if Competitor is present in a concentration comparable to concentration of the substrate, it will bind to active site and enzyme is inhibited by the inactive substrate. There should be much higher concentrations of substance than would be necessary without the competitor to out compete the competitor

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Noncompetitive inhibitor

Is a substance thar forms strong covalent bonds with an enzyme,making it unable to bind with its substrate, and it can not be displaced by the addition of excess substrate.

So noncompetitive inhibition is irreversible

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allosteric inhibition

When noncompetitive inhibition take placed at a site other than the active site, this is called allosteric inhibition

The interaction of an inhibitor at an allosteric site change the structure of the enzyme, so that the active site is also changed.

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Lactase

Lactose to glucose and galactose

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Cofactors

Metal cations Zn 2*, Fe2*

Or coenzyme like as vitamin derivative

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Prosthetic groups

Cofactors that bind to the enzyme by strong covalent bonds are called prosthetic groups.