CH 19 notes Flashcards

(47 cards)

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
Enzyme concentration
if there is plenty of substrate...RXN rate INCREASES linearly w/ enzyme concentration
26
Temperature on enzyme activity
INCREASE in temp INCREASES rate of RXN until temp. gets HIGH enough to DENATURE enzyme..then SHARP DECREASE in activity
27
effect of pH on enzyme activity
each enzyme will have an optimal pH that coincides w. the natural environment of the catalyzed RXn
28
Enzyme activation
any process that INITIATES or increase action of enzyme
29
Enzyme inhibition
any process that SLOWS/ STOPS action of enzyme
30
Feedback Control
regulation of an enzyme's activity by the product of a RXN later in pathway A----(enzym. 1)--> B---(enzym. 2)---> C ---ETC--->
31
Allosteric Control
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
Allosteric Enzyme
enzyme whose activity is controlled by the binging of an activator or inhibitor at location other than active site
33
Uncompetitive Inhibition
enzyme regulation in which inhibitor binds reversibly to the enzyme substrate complex blocks the binding of the second substrate to active site
34
Reversible Competitive Inhibition
enzyme regulation in which an inhibitor competes w/ a substrate for binding to enzyme active site
35
Irreversible Inhibition
enzyme deactivation in which an inhibitor forms covalent bonds for the active site PERMANTELY BLOCKS ACTIVE SITE!!!!!
36
Covalent Modification
removal of addition of an covalently bonded group to modify the activity of enzyme
37
Zygomen
compound that becomes and active enzyme after undergoing a chemical change
38
Genetic (enzyme) control
regulation of enzyme activity by control of the synthesis of enzymes
39
VITAMINS
organic molecule essential in trace amounts MUST BE OBTAINED FROM DIET!!!! cannot be synthesized in body
40
Water- Soluble Vitamins
Must be replaced daily due to solubility in water (urine) MOST ARE COENZYMES ALL B VITS and C-ANTIOXIDANT
41
Vitamin A
ANTIOXIDANT | EYE FUNCTION and SKIN
42
Vitamin D
related to CHOLESTEROL | NEEDED FOR BONE MASS
43
Vitamin E
ANTIOXIDANT PREVENTS form of ANEMIA protects vit A
44
Vitamin K
ESSENTIAL FOR LIVER | prevents BLEEDING DISORDERS (helps blood clot)
45
ANITOXIDANT
substance that prevents oxidation by reacting with an oxidizing agent
46
``` What do VIT C VIT E BETA-CAROTENE MINERAL SELENIUM have in common and what do they do? ```
DIETARY ANTIOXIDANTS work together to defuse the potentially harmful action of free radicals
47
Free Radical
Atom or molecule wit h an unpaired electron wants to attach to anything bad for body