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biology 12 enzymes > enzymes > Flashcards

enzymes Flashcards

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1
Q

what is metabolism

A

a term that describes all the chemical reactions occurring constantly in the cell that maintain homeostasis.

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2
Q

what is metabolic pathways

A

step wise series of chemical reactions from the reactants to the final products.

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3
Q

what are metabolic pathways controlled by

A

enzymes

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4
Q

what is the chemical reaction of cellular respiration?

A

6CO2+6H2O=C6H12O6+ 6O2

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5
Q

why are metabolic pathways needed?

A

not possible to have single reactions that could produce complex molecules from simple reactants. one pathway can lead to several others. lastly, having more than one step means there are more places where the overall reaction can be controlled.

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6
Q

what does an enzyme do

A

a chemical catalyst

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7
Q

what biological molecule is an enzyme

A

protein

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8
Q

what are proteins made up of

A

repeating amino acids

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9
Q

what are enzymes?

A

they are the site of chemical reactions, but they are not used up in the reaction or permanently changed by the reaction.

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10
Q

what is the reactant’s name that is involved in a enzyme’s reaction?

A

substrate

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11
Q

what are the characteristics of enzymes?

A

highly specific and one enzyme only speeds up one reaction.

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12
Q

what is an ES-complex?

A

ES complex stands for enzyme substrate complex, this is formed when the substrate binds to the enzyme at the active site. then the enzyme undergoes a chemical reaction.

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13
Q

where does the substrate bind?

A

active site

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14
Q

does a chemical reaction occur without an ES-complex

A

no there must be a ES-complex so the chemical reaction can occur.

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15
Q

what helps an enzyme

A

co enzyme

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16
Q

what are most co enzymes

A

vitamins

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17
Q

what environmental factors affect the enzyme activity

A

temperature and pH

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18
Q

what is the lock and key theory?

A

the lock and key theory explains how the substrate matches the active site of the enzyme without the active site changing. this is similar to a lock and key because the key has to be the same shape as the lock so the lock can open. if it isn’t the lock doesn’t open.

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19
Q

what is the induced fit theory?

A

the induced fit is when the active site changes shape slightly to create a tighter grip on the substrate.

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20
Q

explain the steps to a enzyme reaction

A

the enzyme and substrate are moving, colliding until they hit one another at the correct energy and angle. the substrate binds with the enzyme’s active site and the chemical reaction occurs. when the product is created the product is released.

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21
Q

what does an enzyme do to the energy?

A

it lowers the activational energy

22
Q

what is activational energy?

A

it is the energy required for an enzyme to begin creating the product

23
Q

how enzymes lower the acitivational energy?

A

by bringing the substrate molecules together and holding them long enough for the reaction to take place.

24
Q

what are enzymes made up of?

A

a protein part that gives it specificity like exactly what reaction it will catalyze and an coenzyme that helps the reaction by accepting or donating atoms.

25
Q

what is a coenzyme?

A

large non protein molecules that are vitamins and helps proceed the reaction.

26
Q

what affect does changing pH have on enzyme activity?

A

removing the enzyme from it’s preferred pH causes the enzyme to start denaturing. when it reaches extreme pH changes it has already denatured. changing the enzyme to more acidic conditions or more basic conditions, add additional hydrogen or hydroxide ions and then it disrupts the bonds between the R groups.

27
Q

what affect does temperature have on enzyme activity?

A

increasing to optimum temperature increases the kinetic energy which increases the collisions between the substrate and the enzyme. the more collisions between these two allows more product to be produced. thus the rate increases. until the optimum temperature. increasing the temperature above the optimum causes the enzyme to denature, it losing shape and the active site changes shape so the substrate can not bind to the active site anymore. if it has lost shape it can not form an ES complex the rate decreases because of the denaturing.

28
Q

what affect does substrate concentration have on enzyme activity?

A

adding more substrate increasing the rate because more substrate is colliding the enzyme and there is higher chances of the enzyme to collide with the substrate. but eventually the rate levels off because the enzyme becomes saturated

29
Q

what affect does enzyme concentration have on enzyme activity?

A

the same affect as adding more substrate,adding more enzyme increasing the rate because more enzyme is colliding substrates and there is higher chances of the substrate to collide with the enzyme. the rate will only level off if the substrate runs out which is usually not the case.

30
Q

what is the preferred pH for most human enzymes

A

6-8

31
Q

what affect does inhibitors have on enzyme activity?

A

adding inhibitors decreases the rate of the reaction

32
Q

what is the optimum temperature or the preferred pH

A

when the enzyme works the best and creates the most amount of product.

33
Q

what is the pH level for trypsin

A

8

34
Q

what is a denatured protein?

A

a denatured protein has lost its normal configuration and therefore it can not form an ES complex.

35
Q

what will happen if we remove enzymes or substrates?

A

it will decrease the rate because if we are removing particles that decreases the chances of the particles to collide with one another.

36
Q

what will happen if we remove enzymes or substrates?

A

it will decrease the rate because if we are removing particles that decreases the chances of the particles to collide with one another. the more particles the better chances of collisions and the increase of production of products.

37
Q

what are inhibitors?

A

inhibitors are molecules that bind to the enzyme some way to prevent or reduce the rate of the substrate binding to the enzyme.

38
Q

what are competitive inhibitors

A

competitive inhibitors are inhibitors that bind to the active site and or prevent the substrate from binding there. this causes the rate to drop because the substrate can not bind there anymore.

39
Q

what is noncompetitive inhibitors

A

these inhibitors bind to another part of the enzyme instead of the active site. but the binding causes the active site to change shapes therefore the substrate can not bind to the active site again because the shape of the active site is not complementary to the substrate.

40
Q

which inhibitors are reversible or irreversible

A

competitive and noncompetitive are both reversible and nonreversible.

41
Q

what does it mean to the enzyme if the inhibitor is reversible.

A

reversible causes the active site to go back to normal and it can start functioning again when the inhibitor leaves.

42
Q

what does irreversible mean to the enzyme if an inhibitor is irreversible?

A

irreversible causes the inhibitor to be attached to it’s active site or where it is bonded

43
Q

does substrate ever run out?

A

running out of substrate is never a case.

44
Q

what is competitive inhibitor the actual definition

A

a molecule that competes for the active site that looks like the substrate

45
Q

if more inhibitors are added what happens to the rate

A

it decreases

46
Q

does the noncompetitive inhibitor look like the substrate

A

it may not look like the the substrate. it may have a complete different shape.

47
Q

what is noncompetitive inhibitors also known as?

A

allosteric inhibition

48
Q

what can inhibitors be

A

chemical that introduced from outside which can act as medicines and poisons

49
Q

what can irreversible inhibitors be

A

HCN hydrogen cyanide

50
Q

what are examples of non competitive inhibitors

A

lead and other heavy metals that cause poisoning when they bind irreversibly and make them denature.

biology 12 enzymes (1 decks)

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