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BIO/BIOCHEM (MCAT) > Biological Molecules and Enzymes > Flashcards

Biological Molecules and Enzymes Flashcards

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MCAT flashcards Biology 101 flashcards
1
Q

allosteric activators

A

binds to the enzymes at a site other than the active site as well as changes the shape of the substrate

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2
Q

allosteric inhibitors

A

binds to the enzymes at a site other than the active site and the substrate can’t bind

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3
Q

adipocytes

A

types of fat cells that have a cytoplasm containing only triglycerides

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4
Q

amphipathic

A

hydrophilic and hydrophobic properties

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5
Q

Cofactors

A

help enzymes reach their optimal activity

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6
Q

Coenzymes

A

are organic molecules that act as cofactors and help catalyze reactions

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7
Q

Enzyme substrate complex

A

this forms when the enzyme binds to the substrate

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8
Q

Fat soluble vitamins

A

vitamins are transported in the body with the fats from one’s diet to help the absorption of said fats; examples are Vitamin A,D,E,K

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9
Q

glycogen

A

a polymer of glucose that contains alpha linkages. found in all animal cells but mostly in the liver and muscle cells

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10
Q

Irreversible inhibitors

A

agents that bind irreversibly to enzymes and interrupt its function

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11
Q

Km

A

refers to how high the concentration of the substrate must be to speed up the reaction

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12
Q

mixed inhibitors

A

bind at a site other than the active site; they can bind to either the enzyme alone or the enzyme-substrate complex

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13
Q

negative cooperativity

A

the first substrate changes the shape of the enzyme but makes the following substrates more difficult to bind

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14
Q

positive cooperativity

A

the first substrate changes the shape of the enzyme, thus making the following substrates more easily able to bind

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15
Q

noncompetitive inhibitors

A

a type of mixed inhibitor that bind noncovalently to an enzyme at a site other than the active site, thus changing the shape of the enzyme

  • no change on Km
  • lower Vmax
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16
Q

oxidoreductases

A

catalyze the transfer of electrons or hydrogen ions

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17
Q

transferases

A

catalyze reactions in which groups are transferred from one place to another

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18
Q

hydrolases

A

regulate hydrolysis

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19
Q

lyases

A

catalyze reactions in which functional groups are added to double bonds or vice versa

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20
Q

isomerases

A

catalyze the transfer of groups within the molecule with the motive of creating isomers

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21
Q

ligases

A

catalyze condensation reactions along with hydrolysis of High energy molecules

22
Q

prostaglandins

A

a group of lipids that are made at the site of tissue damage and infection to resolve injury

23
Q

sphingolipids

A
  • have a long fatty acid chain and polar heads
  • backbone is amino alcohol called sphingosine
    these compounds make up part of the cell membrane
24
Q

starch

A

a type of long term storage that comes in two forms: amylose and amylopectin

25
Q

steroids and example

A
  • a type of lipid with a four-ringed structure

- main example cholesterol

26
Q

cholesterol

A

maintains membrane stability and fluidity as well as acts as a precursor for steroid hormones

27
Q

amylose

A

form of starch - branched or unbranched but has same alpha linkages as glycogen

28
Q

amylopectin

A

form of starch - resembles glycogen but differs in branching structure

29
Q

uncompetitive inhibitors

A

bind to a site other than the active site and once it is bound, the substrate remains associated with that enzyme.

  • Km decreases because affinity for substrate increases
  • Vmax decreases because substrate is bound to enzyme for long time
30
Q

competitive inhibitors

A

binds reversibly to the active site using NON COVALENT bonds and only for a quick second.

  • Km increases
  • Vmax does not change
  • the concentration of the substrate can be increased in order to overcome inhibition
31
Q

Zymogen

A

inactive forms of enzymes that can become irreversibly activated by a change in the environment or other enzymes

32
Q

cytochromes and example

A

proteins that need to have a prosthetic heme group to function
- example is hemoglobin

33
Q

what is the major function of a phospholipid

A

serve as a structural component of membranes

34
Q

what is the major function of triacylglycerols

A

store metabolic energy and provide thermal insulation and padding

35
Q

what is the major function of steroids

A

regulate metabolic activities

36
Q

what is the structure of waxes

A

formed by an ester linkage between a long chain alcohol and a long chain fatty acid

37
Q

what is an advantage of long carbon chains

A

energy storage

38
Q

describe eicosanoids and its three examples mentioned in the book

A

a class of lipids -> released from cell membranes as hormones that regulate BP, body temperature and smooth muscle contraction
examples -> prostaglandins, thromboxanes and leukotrienes

39
Q

what is the important substitution in sickle cell disease

A

an acidic glutamate is replaced with a non polar valine -> causes hemoglobin to polarize

40
Q

what are the five forces that contribute to the tertiary structure

A

covalent disulfide bonds, ionic interactions, hydrogen bonds, van der Waals forces and hydrophobic side chains

41
Q

what are the two types of coenzymes

A

cosubstrates and prosthetic groups

42
Q

what makes an inhibitor competitive

A

when the inhibitor binds to the enzyme’s active site

43
Q

what makes an inhibitor noncompetitive

A

when the inhibitor binds to the enzyme alone or enzyme-substrate complex with the same affinity

44
Q

what makes an inhibitor uncompetitive

A

when the inhibitor only binds to the enzyme-substrate complex

45
Q

define the primary structure of proteins

A

number and sequence of amino acids

46
Q

define the secondary structure of proteins

A

when the single chain forms into distinct shapes -> twist into alpha helices or beta sheets

47
Q

define tertiary structure of proteins

A

three dimensional shape formed by folds of the chain

48
Q

define the quaternary structure of proteins

A

two or more polypeptide chains bind together

49
Q

an enzyme with its cofactor is called….

A

holoenzyme

50
Q

an enzyme without its cofactor is called…

A

apoenzyme

BIO/BIOCHEM (MCAT) (9 decks)

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