ENZYMOLOGY P1 Flashcards

(54 cards)

1
Q

ENZYME CONCENTRATION

A

higher the enzyme concentration, the
faster is the reaction, because more
enzyme is present to the substrate

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2
Q

SUBSTRATE CONCENTRATION

A

With the amount of enzyme exceeding the
amount of substrate, the reaction rate
steadily increases as more substrate is
added
• However, when the substrate
concentration reaches a maximal value,
higher concentration of substrate no
longer results in increased rate of reaction

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3
Q

Enzymes are active at

A

25°C, 30°C, 37°C

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4
Q

optimum temperature for
enzymatic activity

A

37°C

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5
Q

↑temp: __ reaction

A

↑reaction

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6
Q

Rate of denaturation _____ as
temperature increases

A

increases

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7
Q

Temperature that may result to inactivation of enzymes

A

60-65°C

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8
Q

Temperature Coefficient (Q10):

A

every 10°C increase in temp, there will be a 2x increase in enzyme activity

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9
Q

Most reactions occur in pH of

A

7-8

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10
Q

Extreme pH level may cause

A

Denaturation

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11
Q

Low temperatures (refrigeration/freezing)
cause enzyme to be

A

reversibly inactive

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12
Q

Repeated freezing and thawing

A

denaturation

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13
Q

ideal temp. for preservation of
enzymes

A

-20°C

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14
Q

ideal storage temp for substrates
and coenzymes

A

2-8°C

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15
Q

ideal for storage of LDH (LD4 and
LD5)

A

22°C

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16
Q

mostly increases enzyme concentration

A

Hemolysis

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17
Q

mostly decreases enzyme concentration

A

Lactescence or Milky spx.

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18
Q

Shape of substrate (key) must fit into
enzyme (lock)

A

EMIL FISHER’S LOCK AND KEY THEORY

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19
Q

Based on the substrate binding to the
active site of the enzyme

A

KOCHLAND’S INDUCED FIT THEORY

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20
Q

An enzyme combines with one substrate and catalyzes one reaction

A

ABSOLUTE SPECIFICITY

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21
Q

An enzyme combines with substrates
in a chemical group

A

GROUP SPECIFICITY

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22
Q

An enzyme reacting with chemical
bonds

A

BOND SPECIFICITY

23
Q

The reaction rate depends only on
enzyme concentration

A

ZERO-ORDER REACTION

24
Q

The reaction rate is directly
proportional to substrate
concentration

A

FIRST-ORDER REACTION

25
• The reactants are combined • The reaction proceeds for a designated time • The reaction is stopped, and measurement is made
FIXED-TIME
26
• Multiple measurements of change in absorbance made during the reaction • it is preferred than fixed-time
CONTINUOUS MONITORING/KINETIC ASSAY
27
ENZYMES ARE MEASURED IN TERMS OF
1. Change in the substrate concentration 2. Change in the product concentration 3. Change in coenzyme concentration
28
CAUSES OF ELEVATED PLASMA ENZYME LEVELS
1. Impaired removal of enzyme from plasma 2. Impaired permeability of cell membrane 3. Increased in the number of cells or the production of cells 4. Increased in normal cell turnover 5. Decreased clearance of enzymes from the circulation 6. Tissue necrosis and degeneration
29
specific biologic proteins that catalyze biochemical reactions without altering the equilibrium point of the reaction or being consumed or changed in composition
ENZYMES
30
A cavity other than the active site
Allosteric site
31
Forms of an enzyme could be based on physical properties such as
• Electrophoretic mobility • Solubility, or • Resistance to inactivation
32
Fraction of an enzyme
ISOENZYME
33
Necessary for enzyme activity
COFACTOR
34
Inorganic cofactors
ACTIVATOR
35
Organic cofactors
COENZYME
36
Coenzyme bound tightly to the enzyme
PROSTHETIC GROUP
37
Enzyme secreted from the organ of production in a structurally inactive form
ZYMOGEN
38
Prevents an enzymatic reaction to occur
INHIBITOR
39
Physically binds to the active site of an enzyme; reversible
COMPETITIVE INHIBITOR
40
Looks for areas other than the active site; slows the rate of the reaction
NON-COMPETITIVE INHIBITOR
41
The inhibitor binds the enzyme-substrate complex
UNCOMPETITIVE INHIBITOR
42
Assigned systematic name to each enzyme
INTERNATIONAL UNION OF BIOCHEMISTRY
43
FIRST DIGIT
Enzyme Class
44
SECOND AND THIRD DIGIT
Enzyme Sub-Class, Sub-sub-class
45
FOURTH DIGIT
Serial number specific to an enzyme
46
Catalyze an enzyme-reduction reaction between two substrates
OXIDOREDUCTASE
47
Catalyze the transfer of a group other than the hydrogen from one substrate to another
TRANSFERASE
48
Catalyze hydrolysis of various bonds
HYDROLASE
49
Catalyze removal of groups from substrates without hydrolysis
LYASE
50
Catalyze the interconversion of geometric, optical, or positional isomers
ISOMERASE
51
Catalyze the joining of two substrate molecules, coupled with a breaking of the pyrophosphate bond in ATP or similar
LIGASE
52
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