enzymes Flashcards

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

A

cofactor

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

A

cellulase

21
Q

hydrolyzes collagen, promotes burn and would healing

A

collagenase

22
Q

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

A

intertase

23
Q

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

A

lipase

24
Q

hydrolyzes pectin and clarifies fruit juice

A

pectinase

25
Q

hydrolyzes protein and used in detergents

A

protease

26
Q

the maximum possible velocity that a reaction can have at infinite substrate concentration

A

V max

27
Q

the half maximal velocity of a reaction

A

1/2 V max

28
Q

the substrate concentration at which the enzyme has half maximal velocity

A

Km

29
Q

which velocities are the most relevant

A

the initial velocities

30
Q

reaction velocities ____ with time

A

slow down

31
Q

three reasons why enzymes rarely operate at true V max

A

substrate in most cells is not high enough
little or no regulation by substrate at V max
substrate at Km is more realistic

32
Q

an indication of enzyme affinity for substrate

A

Km

33
Q

enzymes with ____ have greater substrate affinity

A

lower Km’s

34
Q

what are the axis for the lineweaver-burk equation graph

A

x axis: 1/substrate conc.

y axis: 1/v

35
Q

the amount of enzyme that produces one mole of product per minute

A

enzyme unit

36
Q

amount of enzyme that produces one mole of product per second

A

katal

37
Q

micromoles of product formed per minute per mg protein

A

specific activity

38
Q

the number of substrate molecules converted to product per unit time by a single molecule of enzyme

A

turnover number (Vmax/[Enz])

39
Q

an estimate of how perfect the enzyme is or how well the enzyme performs when S is low

A

catalytic efficiency (Kcat/Km)