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”

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
removel of CO2 from a substrate
decarboxylases
25
catalyze the arrangemnt of atoms (isomerization) of a substrate in reactions that have 1 sub but 1 product
isomerases
26
2 subclass of isomerases
racemases, mutase
27
catalyze the bonding together of two substrate mol
ligases
28
formation of two substrate bonds with the help of ATP
synthetase
29
formation of new bond from substrate and CO2 with ATP
carboxylase
30
conversion of d-isomer to l-isomer or vice versa
racemases
31
transfer of one functional group from one place to another same molecule
mutase
32
enzyme model in which substrate and enzyme has the same shape
lock and key model
33
enzyme model in which enzyme is flexible to match the shape of the substrate
induced fit model
34
what is absolute specificity of enzyme?
catalyze only 1 reaction
35
linkage specificity ___
enzyme only act on a particular type of bond
36
streochemical specificity
only act on streoisomers
37
group specificity
only act on particular functional group
38
4 types of enzyme specificity
-----
39
maximum number of molecules that one enzyme can accomodate per unit time
turnover number
40
pepsin ____ trypsin ___
acidic and basic
41
it blocks the active site so that no substrate can enter
competitive inhibitor
42
a substrate that only lies on another area of enzyme ( or allosteric site)
incompetitive inhibitor
43
an enzyme that has another site than that of an active site
allosteric enzyme
44
binding of molecule to the other site that affects the binding of a molecule at another site
allosteric control
45
+/- allosteric regulator difference
-----
46
the inhibitor can leave, restoring the enzyme to its uninhibited level of activity
reversible inhibition
47
the inhibitor remains permanently bound and the enzyme is permanently inhibited
irreversible inhibition