enzymes Flashcards

(39 cards)

1
Q

biological catalyst that functions to speed up the rate of a biological reaction, but is not altered or consumed in the reaction

A

enzyme

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2
Q

energy needed for the reaction to go to completion

A

activation energy

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3
Q

the substances upon which an enzyme acts

A

substrates

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4
Q

the substances produced by chemical modification of substrates

A

products

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5
Q

the specific region on/in an enzyme where substrates bind and where the catalytic reaction occurs

A

active site

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6
Q

the unstable “energized” intermediate formed in an enzymatic reaction that has properties of both the substrate and the product

A

transition state

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7
Q

three things enzymes do to lower the activation energy

A

orienting/holding substrates very close together
creating/stabilizing the transition state intermediate
facilitating the reaction via reactive amino acids in the active site

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8
Q

the model that suggests the enzyme active site perfectly matches the shape of the substrate and so the enzyme allows only one substrate to bind to the active site

A

lock and key model

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9
Q

model that suggests substrates fit to active site like a flexible hand in glove, the enzyme-substrate binding changes the shape of both the enzyme and the substrate to fit snugly

A

induced fit model

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10
Q

catalyze oxidation-reduction reactions; add/remove electrons from its substrate

A

oxidoreductases

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11
Q

transfer a functional group from one molecule to another

A

transferases

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12
Q

cleave bonds by adding a water molecule

A

hydrolases

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13
Q

remove functional groups via non-hydrolytic reactions

A

lyases

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14
Q

catalyze rearrangements of functional groups within a molecule

A

isomerases

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15
Q

use the energy from ATP hydrolysis to form bonds between two substrate molecules

A

ligases

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16
Q

EC 1-6

A
  1. oxidoreductases
  2. transferases
  3. hydrolases
  4. lysases
  5. isomerases
  6. ligases
17
Q

loosely bound non-protein components of enzymes that assist in catalytic reactions

18
Q

two main types of cofactor

A

organic and inoganic

19
Q

tightly bound non-protein components of proteins

A

prosthetic groups

20
Q

hydrolyzes cellulose, used as a digestive aid and in biofuel production

21
Q

hydrolyzes collagen, promotes burn and would healing

22
Q

hydrolyzes sucrose, used in the manufacture of soft-centered candy

23
Q

hydrolyzes lipids, used as a digestive aid and improves the flavor of cheese

24
Q

hydrolyzes pectin and clarifies fruit juice

25
hydrolyzes protein and used in detergents
protease
26
the maximum possible velocity that a reaction can have at infinite substrate concentration
V max
27
the half maximal velocity of a reaction
1/2 V max
28
the substrate concentration at which the enzyme has half maximal velocity
Km
29
which velocities are the most relevant
the initial velocities
30
reaction velocities ____ with time
slow down
31
three reasons why enzymes rarely operate at true V max
substrate in most cells is not high enough little or no regulation by substrate at V max substrate at Km is more realistic
32
an indication of enzyme affinity for substrate
Km
33
enzymes with ____ have greater substrate affinity
lower Km's
34
what are the axis for the lineweaver-burk equation graph
x axis: 1/substrate conc. | y axis: 1/v
35
the amount of enzyme that produces one mole of product per minute
enzyme unit
36
amount of enzyme that produces one mole of product per second
katal
37
micromoles of product formed per minute per mg protein
specific activity
38
the number of substrate molecules converted to product per unit time by a single molecule of enzyme
turnover number (Vmax/[Enz])
39
an estimate of how perfect the enzyme is or how well the enzyme performs when S is low
catalytic efficiency (Kcat/Km)