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CHEM 103 > CH 19 notes > Flashcards

CH 19 notes Flashcards

1
Q

Luciferinase

A

Enzyme found in fireflies tails–light production

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2
Q

Catalyst

A

anything that speeds up rate of RXN but itself is unchanged

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3
Q

How does catalyst work?

A

Lowers the energy of the transition state and therefore the activation energy (Ea) of RXN

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4
Q

Enzyme

A

PRO or other molecule that acts as a catalyst for a biochemical RXN

WATER SOLUBLE
GLOBULAR PRO

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5
Q

Active Site

A

pocket in an enzyme w. specific shape and chemical makeup necessary to bind a substrate

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6
Q

Substrate

A

reactant in an enzyme-catalyzed RXN

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7
Q

Specificity enzyme

A

limitation of the activity of an enzyme to a specific substrate, specific RXN, or specific type of RXN

Catalase almost completely specific for decomposition of hydrogen peroxide

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8
Q

Catalysis of enzymes

A

enzymes can also be specific to STEREOCHEMISTRY

catalytic activity of enzyme is measured by its turnover number

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9
Q

Turnover #

A

max # of substrate molecules acted upon by one molecule of enzyme per unit time

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10
Q

Cofactor

A

nonPRO pt of an enzyme that is essential to the enzyme’s catalytic activity, a metal ion of coenzyme

EX:
Fe     Mn
Zn     Mo
Cu    Co
Ni     V
   Se
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11
Q

Coenzyme

A

organic molecule that acts as an enzyme cofactor

certain vitamins are critical building blocks for coenzymes
they’re dietary necessities bc CANT BE SYNTHESIZED IN BODY

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12
Q

Oxidoreductases

A

catalyze redox runs of substrate molecules
usually addition or removal of O2 or H+
must have coenzyme thats either OXIDIZED OR REDUCED

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13
Q

Transferases

A

catalyze transfer of a functional grip form on molecule to another

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14
Q

Hydrolases

A

catalyze the hydrolysis of substrates

EX:
digestion of CHO and PRO

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15
Q

Isomerases

A

catalyze the isomerization (rearrangement of atoms) of a substrate in RXNs that have but one substrate and one product

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16
Q

Lyases

A

Catalyze the addition of a molecule ( H20, CO2, NH3) to a double bond OR reverse RXN in which molecule is eliminated to form a double bond

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17
Q

LIGASES

A

catalyze the bonding together or TWO substrate molecules

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18
Q

Lock and Key

A

historical model

rigid space for rigid piece

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19
Q

Induced- fit model

A

enzyme action

has flexible active site changes shape to accommodate substrate

20
Q

Induced- fit model

Proximity effect

A

joining up of the enzyme with substrate

21
Q

Induced- fit model

Orientation effx

A

holding of substrates at the exact distance and in the exact orientation necessary for a RXn

22
Q

Induced- fit model

Catalytic effx

A

provide ACIDIc, BASIC or other groups required for catalysis

23
Q

Induced- fit model

Energy Effect

A

Lowering energy barrier by induing strain in bonds in the substrate molecule

24
Q

Substrate concentration

A

as substrate concentration increases– rate of RXN INCREASES

starts to level off when the substrates concentration gets high enough that most enzymes are taken

levels off –>add more substrate

25
Q

Enzyme concentration

A

if there is plenty of substrate…RXN rate INCREASES linearly w/ enzyme concentration

26
Q

Temperature on enzyme activity

A

INCREASE in temp INCREASES rate of RXN until temp. gets HIGH enough to DENATURE enzyme..then SHARP DECREASE in activity

27
Q

effect of pH on enzyme activity

A

each enzyme will have an optimal pH that coincides w. the natural environment of the catalyzed RXn

28
Q

Enzyme activation

A

any process that INITIATES or increase action of enzyme

29
Q

Enzyme inhibition

A

any process that SLOWS/ STOPS action of enzyme

30
Q

Feedback Control

A

regulation of an enzyme’s activity by the product of a RXN later in pathway
A—-(enzym. 1)–> B—(enzym. 2)—> C —ETC—>

31
Q

Allosteric Control

A

interaction in which the binding of a regulator at one site on PRO aft the PRO’s ability to bind another molecule at different site

EITHER POSI+IVE (enzyme becomes a better catalyst)
OR NEGATiVe—– (enzyme becomes a less effective catalyst)

32
Q

Allosteric Enzyme

A

enzyme whose activity is controlled by the binging of an activator or inhibitor at location other than active site

33
Q

Uncompetitive Inhibition

A

enzyme regulation in which inhibitor binds reversibly to the enzyme substrate complex

blocks the binding of the second substrate to active site

34
Q

Reversible Competitive Inhibition

A

enzyme regulation in which an inhibitor competes w/ a substrate for binding to enzyme active site

35
Q

Irreversible Inhibition

A

enzyme deactivation in which an inhibitor forms covalent bonds for the active site

PERMANTELY BLOCKS ACTIVE SITE!!!!!

36
Q

Covalent Modification

A

removal of addition of an covalently bonded group to modify the activity of enzyme

37
Q

Zygomen

A

compound that becomes and active enzyme after undergoing a chemical change

38
Q

Genetic (enzyme) control

A

regulation of enzyme activity by control of the synthesis of enzymes

39
Q

VITAMINS

A

organic molecule
essential in trace amounts
MUST BE OBTAINED FROM DIET!!!!
cannot be synthesized in body

40
Q

Water- Soluble Vitamins

A

Must be replaced daily due to solubility in water (urine)
MOST ARE COENZYMES
ALL B VITS and C-ANTIOXIDANT

41
Q

Vitamin A

A

ANTIOXIDANT

EYE FUNCTION and SKIN

42
Q

Vitamin D

A

related to CHOLESTEROL

NEEDED FOR BONE MASS

43
Q

Vitamin E

A

ANTIOXIDANT
PREVENTS form of ANEMIA
protects vit A

44
Q

Vitamin K

A

ESSENTIAL FOR LIVER

prevents BLEEDING DISORDERS (helps blood clot)

45
Q

ANITOXIDANT

A

substance that prevents oxidation by reacting with an oxidizing agent

46
Q 
What do 
VIT C
VIT E
BETA-CAROTENE
MINERAL SELENIUM
have in common and what do they do?
A

DIETARY ANTIOXIDANTS

work together to defuse the potentially harmful action of free radicals

47
Q

Free Radical

A

Atom or molecule wit h an unpaired electron
wants to attach to anything
bad for body

CHEM 103 (4 decks)

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