enzymes Flashcards

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1
Q

what is an enzyme an example of

A

a functional protein

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2
Q

what monomer is enzymes made of

A

amino acids

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3
Q

how do i identify an enzyme by name

A

ends in “ase”

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4
Q

what makes an enzyme

A

polypeptide chains between amino acids

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5
Q

whats the minimum number of amino acids in an enzyme

A

50

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6
Q

what is the primary structure in an enzyme and what bond is involved

A

order of amino acids determined by DNA sequence, with polypeptide bonds between amino acids

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7
Q

what is secondary structure in an enzyme and what bond is involved

A

alpha helixes and beta pleated sheets; form by H-bonds between amino acids.

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8
Q

what is the tertiary structure in an enzyme and what bond is involved

A

3D folding, formed by R-group interactions (ionic, disulfide bridges, hydrophobic)

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9
Q

what is the quaternary structure in an enzyme

A

2 or more polypeptide chains.

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10
Q

what is an enzyme and its function

A

a organic catalyst that speeds up rate of rxn in organic processes by lowering activation energy.

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11
Q

whats activation energy

A

minimum amount of energy needed to start reaction

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12
Q

are enzymes changed or used in a reaction

A

no

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13
Q

what quantities are enzymes effective in

A

minute quantities

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14
Q

why are enzymes specific

A

because they can only catalyze one substance, and this substance is called a substrate.

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15
Q

what do cofactors and coenzymes do

A

increase rate of enzyme in catalyzed reaction

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16
Q

what are coenzymes

A

organic molecules that are required by certain enzymes to carry out the chemical reaction

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17
Q

how do coenzymes work

A

attach to enzyme and allow substrate to bond and reaction occurs (ex. Vitamin D)

18
Q

what are cofactors often classified as

A

metal ion substances (ex. Fe)

19
Q

what do inhibitors do

A

slow rate of reaction in enzyme catalyzed reaction

20
Q

what is a irreversible inhibitor

A

one that bonds to the enzyme and doesnt come off, permanently blocking it (ex. lead)

21
Q

what is a reversible inhibitor

A

one that forms a temporary bond and slows the rate of rxn while bound. it can be overcome by adding more substrates.

22
Q

what does the attaching and removing of a reversible inhibitor create

A

feedback that allows for normal body regulation. increasing a substance stimulates release, and inhibiting it decreases the amount. this allows for us to stay in the small range of homeostasis.

23
Q

what are competitive inhibitors.

A

inhibitors that closely match the substrate and compete for the active site with the substrate. it lowers the likelyhood of a enzyme binding to a substrate, decreasing overall rate of reaction

24
Q

whats an example of a competitive inhibitor

A

antibiotics

25
Q

how does ph relate to enzymes

A

enzymes can only function optimally at a certain pH, and will denature as it deviates from that. a change in pH leads to breaking bonds that hold the tertiary structure of the enzyme together.

26
Q

whats the optimal temperature for most enzymes, and what happens if you go past it or before it.

A

37c or 98.6 F. if you go past it, the enzyme will start to denature. if you go before it, the enzyme’ rate of reaction will slow down

27
Q

what is substrate concentration

A

when there is a fixed amt of enzyme and increasing amount o substrate.

28
Q

what happens when substrate concentration is increased

A

rate of reaction increases until it hits the optimum rate. after this point, it’ll stay constant unless more enzymes are added. as it increases, the enzyme becomes saturated

29
Q

whats a saturated enzyme

A

when all enzymes are engaged in a ES complex

30
Q

whats enzyme concentration

A

when theres a fixed amt of substrate but an increasing amt of enzyme

31
Q

what happens as enzyme concentration increases

A

rate of reaction increases rapidly then levels off unless more substrates are added

32
Q

whats ES complex

A

when an enzyme and substrate combine and start a reaction

33
Q

whats a metabolic pathway

A

1 sequence of enzymatic reactions

34
Q

whats a metabolism

A

sum of all the chemical processes in an organism

35
Q

what 2 factors can be used to speed p enzymatic reactions

A

increasing temp before optimum, increasing substrate and enzyme concentration

36
Q

what three factors can lead to denaturing of enzymes

A

changing pH level, increasing temp past optimum, irreversible inhibitor, non-comp inhibitor

37
Q

what is an allosteric enzyme

A

one that has two sites; a active and regulatory site. non-competitive inhibitors can bind with the regulatory site to either enable or shut down the reaction. these are called activators and repressors respectively.

38
Q

what is feedback inhibition

A

when the product of a reaction gives feedback, and allows for regulation of the reaction, via turning it on or off.

39
Q

whats a anabolic reaction

A

a reaction in which bonds are formed (dehydration synthesis)

40
Q

what is a catabolic reaciton

A

a reaction in which bonds are broken (digestion, hydrolysis, cell respiration)

41
Q

whats an exorgenic reaction

A

a catabolic reaction where energy is released, and bonds are broken. it is spontaneous

42
Q
A