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Biochemistry > Enzymes and Vitamins > Flashcards

Enzymes and Vitamins Flashcards

1
Q

What is an Enzyme?

A

protein that acts as a catalyst for a biochemical reaction.

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2
Q

These are the two enzyme structures (describe their differences)

A

Simple (composed only of protein) and Conjugated Enzyme (has a
nonprotein part in addition to a
protein part)

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3
Q

Apoenzyme + Cofactor = ?

A

Holoenzyme

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4
Q

protein part of conjugated enzyme

A

apoenzyme

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5
Q

NON protein part of conjugated enzyme

A

cofactor

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6
Q

what is the function of a catalysts?

A

speeds up chemical reaction and does not undergo any changes at the end

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7
Q

suffix of an enzyme

A

-ase

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8
Q

an enzymes’ prefix is often noted by its _____

A

type of reaction that it catalyzes

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9
Q

a catalyze oxidation-reduction that adds or removes an oxygen or hydrogen

A

Oxidoreductases

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10
Q

subclass of Oxidoreductases and their functions

A

Oxidases - oxidation of a substrate
Reductases - reduction of a substrate
Dehydrogenases - removal of two H atoms from a substrate

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11
Q

it catalyze transfer of one group to another

A

transferases

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12
Q

subclass of transferases and their functions between substrates

A

transaminase - Transfer of amino group between substrates
kinase - Transfer of a phosphate group between substrates

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13
Q

catalyze the hydrolysis of substrate

breaking of bonds and addition of water

A

hydrolases

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14
Q

hydrolysis in ester linkages in LIPIDS

A

lipases

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15
Q

hydrolysis of AMIDE LINKAGES in proteins

A

proteases

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16
Q

hydrolysis of GLYCOSIDIC BONDS of carbohydrates

A

carbohydrases

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16
Q

hydrolysis of SUGAR-PHOSTPHATE ester bond in carbohydrates

A

nucleases

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17
Q

hydrolysis of PHOSTPHATE ester bond

A

phosphatases

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18
Q

“lein” word means?

A

to break

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19
Q

it catalyze the addion of hydrogen oxiden or carbon dioxide to a double bond/reverse rection in which a molecule is eliminated to leave a double bond
“to break”

A

lyases

20
Q

the 4 subclass of lyases

A

dehydratases, decarboxylases, deaminases, hydratases

21
Q

addition of H2O from a substrate

A

hydratases

22
Q

removel of NH3 from a substrate

A

deaminases

23
Q

removal of H2O from a substrate

A

dehydratases

24
Q

removel of CO2 from a substrate

A

decarboxylases

25
Q

catalyze the arrangemnt of atoms (isomerization) of a substrate in reactions that have 1 sub but 1 product

A

isomerases

26
Q

2 subclass of isomerases

A

racemases, mutase

27
Q

catalyze the bonding together of two substrate mol

A

ligases

28
Q

formation of two substrate bonds with the help of ATP

A

synthetase

29
Q

formation of new bond from substrate and CO2 with ATP

A

carboxylase

30
Q

conversion of d-isomer to l-isomer or vice versa

A

racemases

31
Q

transfer of one functional group from one place to another same molecule

A

mutase

32
Q

enzyme model in which substrate and enzyme has the same shape

A

lock and key model

33
Q

enzyme model in which enzyme is flexible to match the shape of the substrate

A

induced fit model

34
Q

what is absolute specificity of enzyme?

A

catalyze only 1 reaction

35
Q

linkage specificity ___

A

enzyme only act on a particular type of bond

36
Q

streochemical specificity

A

only act on streoisomers

37
Q

group specificity

A

only act on particular functional group

38
Q

4 types of enzyme specificity

A
39
Q

maximum number of molecules that one enzyme can accomodate per unit time

A

turnover number

40
Q

pepsin ____ trypsin ___

A

acidic and basic

41
Q

it blocks the active site so that no substrate can enter

A

competitive inhibitor

42
Q

a substrate that only lies on another area of enzyme ( or allosteric site)

A

incompetitive inhibitor

43
Q

an enzyme that has another site than that of an active site

A

allosteric enzyme

44
Q

binding of molecule to the other site that affects the binding of a molecule at another site

A

allosteric control

45
Q

+/- allosteric regulator difference

A
46
Q

the inhibitor can leave, restoring the enzyme to its
uninhibited level of activity

A

reversible inhibition

47
Q

the inhibitor remains permanently bound and the
enzyme is permanently inhibited

A

irreversible inhibition

Biochemistry (14 decks)

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