enzymes Flashcards

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
how does ph relate to enzymes
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
whats the optimal temperature for most enzymes, and what happens if you go past it or before it.
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
what is substrate concentration
when there is a fixed amt of enzyme and increasing amount o substrate.
28
what happens when substrate concentration is increased
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
whats a saturated enzyme
when all enzymes are engaged in a ES complex
30
whats enzyme concentration
when theres a fixed amt of substrate but an increasing amt of enzyme
31
what happens as enzyme concentration increases
rate of reaction increases rapidly then levels off unless more substrates are added
32
whats ES complex
when an enzyme and substrate combine and start a reaction
33
whats a metabolic pathway
1 sequence of enzymatic reactions
34
whats a metabolism
sum of all the chemical processes in an organism
35
what 2 factors can be used to speed p enzymatic reactions
increasing temp before optimum, increasing substrate and enzyme concentration
36
what three factors can lead to denaturing of enzymes
changing pH level, increasing temp past optimum, irreversible inhibitor, non-comp inhibitor
37
what is an allosteric enzyme
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
what is feedback inhibition
when the product of a reaction gives feedback, and allows for regulation of the reaction, via turning it on or off.
39
whats a anabolic reaction
a reaction in which bonds are formed (dehydration synthesis)
40
what is a catabolic reaciton
a reaction in which bonds are broken (digestion, hydrolysis, cell respiration)
41
whats an exorgenic reaction
a catabolic reaction where energy is released, and bonds are broken. it is spontaneous
42