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cell biology > enzymes > Flashcards

enzymes Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

what is a cofactor?

A

non-protein component of an enzyme required for activity

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2
Q

what is a prosthetic group?

A

non-dissociable cofactor

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3
Q

what is a co-enzyme?

A

dissociable cofactor

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4
Q

what is an apoenzyme?

A

enzyme without a cofactor

inactive

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5
Q

what is a holoenzyme

A

enzyme with a cofactor

active

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6
Q

what is heme

A

enzyme cofactor

porphyrin ring with iron

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7
Q

what are the precursors of cofactors and coenzymes?

A

vitamins

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8
Q

what does a lack of B1 cause?

A

Beriberi

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9
Q

what does a lack of vitamin B3 cause?

A

pellagra

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10
Q

what are proenzymes?

A

inactive form of enzymes

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11
Q

how are proenzymes activated?

A

proteolytic conversion which is irreversible

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12
Q

what are common proenzymes?

A

digestive enzymes
blood clotting enzymes
developmental enzymes

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13
Q

what is the prefix of proenzymes?

A

-ogen

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14
Q

what is chymotripsinogen?

A

proenzyme synthesised in the pancreas

activated by cleaving peptide bonds

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15
Q

how is chymotripsinogen activated?

A

trypsin cleaves bonds to remove a dipeptide (14 and 15)

another dipeptide 147 and 148 are removed

forms A-chymotrypsin which are three chains interconnected by disulphide bonds

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16
Q

what is the michaelis-menten equation?

A

explains the relationship between rate of reaction and substrate concentration

V0 = Vmax[S]/Km + S

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17
Q

what is the michaelis constant?

A

substrate concentration when the reaction rate is half of Vmax

18
Q

what does the michaelis constant show?

A

a measure of enzyme activity

19
Q

what does a high michaelis constant show?

A

enzyme has a low affinity for the substrate - lots is needed for it to reach Vmax/2`

20
Q

what are isoenzymes?

A

different forms of one enzyme catalysing the same reaction (but in different tissues)

21
Q

give an example of an isoenzyme

A

lactate dehydrogenase

22
Q

name methods that energy can be stored and released

A 
ATP
phosphocreatinine
other nucleotides - GTP
carbohydrates and glycogen
fat
23
Q

describe the structure of ATP

A

ribose
adenine
three phosphates

24
Q

how is phosphocreatine made?

A

phosphorylation of creatine using ATP catalysed by creatine kinase

25
Q

what are the uses of biological energy?

A

transport
motility
anabolism
heat

26
Q

what is an absolute enzyme?

A

catalyses one type of reaction for a single substrate

27
Q

what is a group enzyme?

A

catalyses one type of reaction for a group of substrates

28
Q

what is a linkage enzyme?

A

catalyses one type of reaction for a specific type of bond

29
Q

what do oxidoreductases do?

A

oxidation and reduction reactions

30
Q

what do transferases do?

A

transfer of functional groups

31
Q

what do hydrolases do?

A

hydrolysis

32
Q

what do lyases do?

A

add/remove groups from double bond without oxidation or reduction

33
Q

what do isomerases do?

A

rearrange atoms to form isomers

34
Q

what do ligases do?

A

bond molecules using ATP

35
Q

how is trypsinogen stored?

A

acinar cells

36
Q

where is chymotrypsinogen cleaved?

A

in the duodenum

37
Q

what is the reaction rate V?

A

no of reactions/second catalysed per molecule of the enzyme

38
Q

what is malonate?

A

competitive reversible inhibitor of succinate dehydrogenase

39
Q

what is irreversible inhibition?

A

an irreversible inhibitor destroys enzyme activity, usually by bonding with side-chain groups in the active site

40
Q

what is a non-competitve inhibitor?

A

has a structure different to the substrate

binds to somewhere that isnt the active site and changes the shape of the active site so the substrate cant bind

41
Q

what is an uncompetitive inhibitor?

A

has a shape different to the substrate

binds to the ES complex so less product is formed and the ES dissociates slowly

cell biology (17 decks)

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