Enzymes Flashcards

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1
Q

enzymes are ….. proteins

A

globular

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2
Q

ribozymes

A

catalytic RNA molecules with no protein component

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3
Q

apoenzymes

A

protein component

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4
Q

holoenzymes

A

whole enzyme

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5
Q

active site

A

where the substrate binds

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6
Q

enzyme functions

A

lower activation energy

increase rate of spontaneous reactions

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7
Q

addition of an enzymes lower the

A

activation energy

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8
Q

delta G =

A

Delta H - T delta S

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9
Q

enzymes form non-covalent bonds with substrate molecules called the

A

binding energy

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10
Q

binding energy allows the enzymes to

A

take the reaction through a different path of reaction intermediates

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11
Q

how do enzymes reduce the activation energy?

A

entropy reduction

desolvation

induced fit

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12
Q

desolvation

A

weak bonds between substrate and enzymes replaced with H bonds

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13
Q

Vo

A

initial velocity

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14
Q

low substrate concentration gives you an

A

increase in Vo

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15
Q

when [S] becomes so large that Vo changes are vanishingly small you get

A

maximum reaction velocity

Vmax

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16
Q

E + (K1) gives ES which gives

A

E + P (k2)

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17
Q

K1 is a ……….. reaction

A

reversible

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18
Q

K2 occurs ………. than K1

A

slower

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19
Q

Study of initial rates of reaction are termed

A

steady state kinetics

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20
Q

Rate limiting step of enzymatic reactions is the breakdown of

A

ES complex to give free enzymes and product

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21
Q

Half of Vmax is

A

michealis constant

22
Q
the
substrate concentration at
which the initial reaction
rate is half of the maximum
reaction rate
A

Km

23
Q

the ratio of rate constant for breakdown of ES to E + S compared to the rate constant for formation of ES from E + S

A

Km

24
Q

Larger Km indicates a

A

less stable ES complex

25
Q

Smaller Km indicates a

A

more stable ES complex

26
Q

Km indicates the ……. for a substrate

A

affinity

27
Q

Glucose + ATP =

A

glucose-6-phosphate + ADP

28
Q

Glucokinase and hexokinase catalyse

A

glucose to glucose 6 phosphate

29
Q

Glucokinase Km and Vmax are both

A

high

30
Q

Hexokinase Km and Vmax are both

A

low

31
Q

what increases after a meal

A

glucokinase

32
Q

when blood glucose is low - it is released from the liver via

A

gluconeogenesis

33
Q

when blood sugar levels are low

A

Glucokinase also low

34
Q

isoenzymes

A

different enzymes that catalyse the same reaction

35
Q

hexokinase is in

A

muscle

36
Q

Glucokinase is in the

A

liver

37
Q

electrophoresis is useful to

A

separate plasma protein

38
Q

elevation of CK2 indicates

A

myocardial infarction

39
Q

Catalysing reaction with two or more substrates usually involved

A

transfer of groups from one substrate to the other

40
Q

In an ordered sequential reaction mechanism the enzyme exists in a ………….. structure

A

ternary

41
Q

Lactate dehydrogenase catalyses

A

pyruvate to lactate

co enzyme needed: NADH

42
Q

example of random sequential mechanism

A

phosphocreatine from creatine

43
Q

Allosteric enzymes are made up of

A

many subunits, which contain many active sites

44
Q

3 things that can change the way an enzyme functions

A

temperature

pH

inhibitors

45
Q

feedback inhibition

A

build up at the end product of a pathway can slow the entire pathway

46
Q

allosteric effectors bind to a site that is not the ……….. which changes the enzymes structure

A

active site

47
Q

allosteric enzymes

concerted model

A

each subunit exists in two different conformations

one binds substrate and the other doesn’t

48
Q

allosteric enzymes

sequential model

A

no flipping between conformation sites

substrate binding causes a change in ONE subunit

49
Q

Different ways inhibitors can effect enzymes

A

Competitive inhibitor

Non-competitive inhibitor

Irreversible inhibitor

Feedback inhibition

50
Q

Proproteins can be cleaved to give active enzyme by

A

proteases