*5* Micro Metabolism

Front 1

Metabolism

Back 1

The sum of all chemical reactions that occur within a living organism.

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Anabolism

Back 2

Synthesis of chemical compounds (combine simpler substances into more complex molecules.) Requires energy (endergonic) e.g. Protein from amino acid.

Front 3

Catabolism

Back 3

Break down of complex compounds into simpler ones. Releases energy. (exergonic)

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True

Back 4

Most metabolism requires energy.

T/F

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Enzymes

Back 5

Biological catalyst (speeds up reactions) (unaltered by reaction) A specialized protein that speeds up a reaction without being altered by the reaction.

Front 6

catalyst

Back 6

Biological ___________

A specialized protein that speeds up a reaction without being altered by the reaction.

Front 7

Enzymes lower the "Activation energy"

Back 7

What is the mechanism for enzyme action?

Front 8

"Activation energy"

Back 8

the amount of energy to get it going.

Front 9

Active site

Back 9

Gives the enzyme it specificity. Where it binds to the substrate.

Front 10

substrate

Back 10

Active site binds with the _________ to form an enzyme-substrate complex.

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enzymes

Back 11

Some _______ are protein only, others have a protein and a nonprotein portion.

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Apoenzyme

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The protein portion of the enzyme is called ____________.

Front 13

Cofactor

Back 13

What is the nonprotein portion of the enzyme called?

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Coenzyme

Back 14

What is the organic cofactor portion of the enzyme called?

Front 15

holoenzymes

Back 15

Apoenzymes + Cofactor = ____________.

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"lock and key" fit

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Enzymes only react w/ a specific substrate.

Front 17

Specificity

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__________ is due to surface configuration/conformation (shape) of the protein.

Front 18

Primary, Secondary, Tertiary and Quaternary structure

Back 18

What is the conformation (shape) the result of in enzyme structure?

Front 19

Weak interactions

(hydrogen bonds, ionic bonds, and hydrophobic interactions.)

Back 19

What holds the enzymes together?

Front 20

Hydrogen bonding
Ionic bonds
Hydrophobic interactions

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What are the names of the weak interactions in enzymes?

Front 21

Hydrogen bonding

Back 21

holds pleated sheet together.

Front 22

Ionic bonds

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+ and -

opposite charges attract during this bond.

Front 23

Hydrophobic interactions

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Water hating interactions

nonpolar R groups.

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Covalent linkage

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Disulfide bridges btwn two cysteine monomers.
Disulfide bonds
In addition to conformation specificity involves ionic character.

Front 25

ionic character.

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In addition to conformation specificity involves _____ __________.

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Disulfide

Back 26

_________ bridges btwn two cysteine monomers.

Front 27

Denaturing of enzymes by temp or pH
Substrate concentration
Competitive inhibition
Noncompetitive inhibition
Feedback inhibition

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What are the factors influencing enzyme activity?

Front 28

Substrate concentration

Back 28

AkA saturation
There is a max rate at which a certain amount of enzyme can catalyzed a specific reaction.

as an increase in substrate, it plateus.

Front 29

Competitive inhibition

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competition btwn inhibitor and true substrate for they bind at the active site, and the enzyme can no longer bind correctly or not at all.

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Noncompetitive inhibition

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they bind to the allosteric sites on the enzyme.

e.g. poisons.

Front 31

Feedback inhibition

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This control mechanism stops the cell from wasting chemical resources by making more of a substance than it needs.

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Noncompetitive inhibitors

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do not compete with the substrate for the enzymes active site; instead, they interact with another part of the enzyme called the allosteric site.

This causes the active site to change its shape and become nonfunctional.

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Exoenzyme/Extracellular enzymes

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Function outside the cell. (enzyme)

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Endoenzymes/Intracellular enzymes

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Enzyme that functions inside the cell.

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Energy

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The capacity to do work.

Front 36

Kinetic
Potential

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What are the two states of energy?

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Kinetic energy

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The energy of motion.

Front 38

Potential energy

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Energy which is stored (inactive).

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1st law of thermodynamics

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Energy is conserved

Energy cannot be created or destroyed, but can be transformed: changed from one form to another.

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2nd law of thermodynamics

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In any change of energy from one form to another entropy (disorder) increases. Some of the energy becomes unavailable to do work.

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Entropy

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a measure of the degreee of disorder or randomness of a system.

Front 42

energy

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To maintain life (a complex ordered system) cells need a constant source of _______.

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Oxidation and Reduction reactions

Back 43

Electrons are transferred from one atom to another.

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oxidized

(oil)

Back 44

Atoms that lose electrons are "________"

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reduced

(rig)

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Atoms that gain electrons are "_________".

Front 46

hydrogen

Back 46

In the oxidation-reduction reaction, in biological systems, the electrons are often associated with ___________ atoms.

Front 47

Biological oxidations

Back 47

_________ __________ are often dehydrogenations.

Front 48

ATP

Back 48

In oxidation-reduction, organisms concentrate (stored energy)energy in the high energy bonds of _____.