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BIO150 > Enzymes > Flashcards

Enzymes Flashcards

1
Q

all chemical reactions that occurs within an organism

A

metabolism

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2
Q

simpler substance combined to form complex substances

- endergonic reaction

A

anabolism-

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3
Q
  • complex substance broken down to form simpler substance

- exergonic reaction

A

catabolism

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4
Q

example of anabolism

A

synthesis of glycogen

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5
Q

example of catabolism

A

hydrolysis of glycogen

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6
Q

function of catalyst

A

speed up chemical reaction but stay unchanged at the end of the reaction

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7
Q

6 characteristics of an enzyme

A

has catalytic properties, specific active site, reversible reaction, enzyme specificity, very efficient, affected by many factors

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8
Q

types of enzyme specificity

A

absolute specificity, group specificity, linkage specificity

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9
Q

absolute specificity

A

catalyze only one reaction

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10
Q

act only on specific functional group.

eg; amino, methyl, phosphate

A

group specificity

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11
Q

act on particular type of chemical bond

A

linkage specificity

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12
Q

how does an enzyme speed up chemical reactions?

A

by lowering the activation energy

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13
Q
  • unstable condition
  • substrate activated; breaking and making bonds can occur
  • increases the chances of successful collision
A

what happens at transition state

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14
Q

energy is released
ΔG < 0
reactants > products

A

exergonic reaction

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15
Q

energy is absorbed
ΔG > 0
reactants < products

A

endergonic reaction

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16
Q

energy generated by catabolic process used by cells to perform anabolic process

A

energy coupling

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17
Q

how to lower the activation energy

A
  • orienting substrates correctly
  • straining substrate bonds
  • provide favorable microenvironment
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18
Q

the active site in the enzyme has a fixed, rigid and geometrical conformation

A

lock & key model

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19
Q

active site changes shape so that substrate can fit into it

A

induced fit

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20
Q

only substrate with complementary shape can accommodate the site

A

lock & key model

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21
Q

substrate with non-complementary shape can accommodate the site

A

induced fit

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22
Q

active site will return to its original shape when the product is released

A

induced fit

23
Q

6 factors influencing enzyme activity

A

pH value, temperature, substrate concentration, enzyme concentration, cofactor, inhibitor

24
Q

below optimum temperature

A

reaction will increase as the temperature increases until it reaches the optimum temperature

25
Q

above optimum temperature

A

enzyme will be denatured and lose its catalytic properties

26
Q

atom in enzyme will vibrate violently, breaking the bonds which held the enzyme in shape.

A

above optimum temperature

27
Q

enzyme concentration

A

reaction will increase as the enzyme concentration increases

28
Q

rate of reaction increases with increasing substrate concentration up to the

A

point of saturation.

29
Q

2 types of inhibition

A

reversible & irreversible inhibition

30
Q

molecules will bind permanently with the enzyme by covalent bond

A

irreversible inhibition

31
Q

cyanide, insecticide is the example of molecules for

A

irreversible inhibition

32
Q

2 types of reversible inhibition

A

competitive & non-competitive(allosteric site) inhibitor

33
Q

has a similar shape to natural substrate and fits temporarily on active site

A

competitive inhibition

34
Q

no structural similarities to natural substrate and attached to allosteric site

A

non-competitive inhibition

35
Q

effect can be reduced if substrate concentration increases

A

competitive inhibition

36
Q

effect cant be reduced if substrate concentration increases

A

non-competitive inhibition

37
Q

malonic acid molecule is the inhibitor for

A

competitive inhibition

38
Q

amino acid isoleucine is the inhibitor for

A

non-competitive inhibition

39
Q

example of enzyme cofactor

A

inorganic ion, prosthetic group, coenzymes

40
Q

non protein components that are bound tightly or loosely required for certain enzymes for their efficient activity

A

enzyme cofactors

41
Q

attaches temporarily

eg; zink, chlorine

A

inorganic ions

42
Q

binds tightly and permanently

eg; FAD

A

prosthetic group

43
Q
  • binds loosely and temporarily
  • obtained from vitamins
  • eg; NAD+
A

coenzymes

44
Q

enzyme-protein portion

A

apoenzyme

45
Q

a non protein component

A

cofactor

46
Q

apoenzyme + cofactor =

A

haloenzyme

47
Q

a molecule that binds to an enzyme at a site other than the active site and change the enzyme activity

A

allosteric regulation

48
Q

6 classes of enzymes

A

hydrolase, oxidoreductase, transferase, lyase, isomerase, ligase

49
Q
  • formation of 2 products from a substrate by hydrolysis

- lipase, amylase

A

hydrolase

50
Q
  • non-hydrolytic addition or removal of groups from substrates
  • aldolase
A

lyases

51
Q
  • rearrangement of atoms within a molecule

- glucose-phosphate isomerase

A

isomerase

52
Q
  • join together 2 molecules by the break down of ATP

- phosphokinase

A

ligases

53
Q
  • transfer of a functional group from one substance to another
  • transaminase kinase
A

transferase

54
Q
  • involved in oxidation and reduction

- cytochrome oxidose

A

oxidoreductase

BIO150 (14 decks)

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