THE ROLE OF ENZYMES ENZYMES ARE “BOSSY” PROTEINS.

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THE ROLE OF ENZYMES ENZYMES ARE “BOSSY” PROTEINS

Transcript of THE ROLE OF ENZYMES ENZYMES ARE “BOSSY” PROTEINS.

Page 1: THE ROLE OF ENZYMES ENZYMES ARE “BOSSY” PROTEINS.

THE R

OLE O

F

ENZYMES

ENZYM

ES ARE “

BO

SSY”

PRO

TEINS

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ENZYMES ARE PROTEINS!

Enzymes have names that often end in the suffix “-ase.”

FOR EXAMPLE:

LIPASE breaks down LIPIDS

MALTASE breaks down MALTOSE

PROTEASE breaks down PROTEINS

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ENZYMES REACT WITH ONLY ONE (1) TYPE OF MATERIAL. THIS IS CALLED A SUBSTRATE.

The SUBSTRATE has a SHAPE that “FITS” together with the shape of the enzyme.

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THE SHAPE ON THE SURFACE OF THE ENZYME IS CALLED THE ACTIVE SITE.

Notice that the SUBSTRATE has a shape that will “FIT” together with the ACTIVE SITE of the ENZYME. Together they will form an ENZYME-SUBSTRATE COMPLEX.

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ENZYME-SUBSTRATE COMPLEX

The enzyme-substrate complex is TEMPORARY.

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ENZYME FUNCTION

• Enzymes control the RATE of chemical reactions. That means that they SPEED UP the reaction WITHOUT BEING CHANGED!

• Enzymes act as ORGANIC CATALYSTS. They lower the amount of energy needed for a reaction to occur.

• Enzymes are NOT changed by the reaction so they can be used over again and again and again….

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LOCK AND KEY MODEL OF ENZYME ACTION

If the KEY doesn’t have a SHAPE that FITS with the LOCK, then it will not open the lock.

If the ENZYME and SUBSTRATE don’t FIT together, a REACTION will NOT occur.

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ENZYMES DO NOT CHANGE!!

After a reaction is over, the SUBSTRATE is changed, but the ENZYME remains the same.

Notice that the substrate was changed at the end of the reaction.

A - Enzyme

B – Active Site

C - Substrate

D – Enzyme-Substrate Complex

E – Enzyme

F - Products

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SYNTHESIS

(Build up)

Makes COMPLEX substances by joining simple ones together

HYDROLYSIS

(Break down)

Sometimes called

DIGESTION!Breaks complex

molecules into smaller, simple ones

THERE ARE TWO (2) KINDS OF ENZYME-CONTROLLED REACTIONS:

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SYNTHESIS

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HYDROLYSIS

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HYDROLYSIS REACTION VIDEO

http://youtu.be/b7TdWLNhMtM

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