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cee cee 2 finals > Classification, Nomenclature and Kinetics > Flashcards

Classification, Nomenclature and Kinetics Flashcards

1
Q

In enzyme commission numerical code, the nomenclature always starts with E.C. followed by the four digits.

Explain the representation of each digit: (1-4)

A
  • First digit- represents enzyme’s class
  • Second digit- represent enzyme’s subclass
  • Third digit- represent enzyme’s sub subclass
  • Fourth digit- represent enzyme’s serial number specific to the enzyme sub subclass
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2
Q

Enumerate the classification of enzymes in order: (6)

A
  1. Oxidoreductase
  2. Transferase
  3. Hydrolase
  4. Lyase
  5. Isomerase
  6. Ligase
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3
Q

these enzymes catalyze redox reaction between substrates; these enzymes utilize
coenzymes

A

Oxidoreductase

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4
Q

Enzymatic reaction of Oxidoreductase

A

A- + B → A + B-

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5
Q

enzymes that catalyze the transfer of specific chemical group other than hydrogen ions
between substrates

A

Transferase

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6
Q

specific type of transferase that would catalyze the transfer of phosphate group from one substrate to another

A

Kinase

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7
Q

Enzymatic reaction of Transferase

A

A-X(chemical grp) + B → A + B-X

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8
Q

these are enzymes that catalyze the hydrolysis of various chemical bonds

A

Hydrolase

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9
Q

Requirement in order for Hydrolase to function

A

there must be water in able to function

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10
Q

Enzymatic reaction of Hydrolase

A

A–B + H2O → A–OH + B–H

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11
Q

enzymes that catalyze the removal of chemical groups from substrates without hydrolysis

A

Lyase

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12
Q

In lyase, the product retains what type of bond?

A

Double bond

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13
Q

Enzymatic reaction of Lyase

A

ATP → cAMP + PPi

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14
Q

Enzymes that catalyze the interconversion of the geometric optical and positional isomers;
would catalyze the interconversion of substrate A to become substrate B

A

Isomerase

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15
Q

Enzymatic reaction of Isomerase

A

A → B

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16
Q

enzymes that catalyze the joining of two substrate molecules coupled with the breaking of
pyrophosphate bond in ATP

A

Ligases

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17
Q

Enzymatic Reaction of Ligase

A

Ab + C → A–C + b

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18
Q

Enzymes catalyze physiologic reactions by increasing the activation energy level that the reactants must reach. The greater the required activation energy the longer the reaction to proceed.

a. First statement is true, second statement is true.
b. First statement is false, second statement is true.
c. First statement is true, second statement is false.
d. First statement is false, second statement is false.

A

b. First statement is false, second statement is true.

Enzymes catalyze physiologic reactions by DECREASING/LOWERING the activation energy level that the reactants must reach

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19
Q

The lower the activation energy required the slower the formation of the product

a. True
b. False

A

b. False

Lower activation energy = faster formation of product

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20
Q

In catalytic mechanism of enzymes, relationship between enzymes, substrate, and product occurs.

Enumerate the relationship/specificity of enzymes: (4)

A
  1. Absolute specificity
  2. Group specificity
  3. Bond specificity
  4. Stereoisomeric specificity
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21
Q

Relationship between enzymes, substrate, and product:

Explain absolute specificity

A

Enzymes combined with only one substrate and catalyze only one corresponding reaction

22
Q

Relationship between enzymes, substrate, and product:

Explain group specificity

A

enzymes combined with all substrates containing a particular group

23
Q

Relationship between enzymes, substrate, and product:

Explain bond specificity

A

enzyme reaction is specific to chemical bonds

24
Q

Factors that Influence Enzymatic Reactions: (7)

A
  1. Substrate Concentration
  2. Enzyme Concentration
  3. pH
  4. Temperature
  5. Cofactors
  6. Storage
  7. Hemolyzed samples
24
Q

Relationship between enzymes, substrate, and product:

Explain stereoisomeric specificity

A

enzymes that combined with only one optical isomer

25
Q

Reaction rate is proportional to the substrate concentration with the activity

a. Zero-order kinetics
b. First order kinetics

A

b. First order kinetics

26
Q

Only a fixed number of substrate (in excess) is converted to product per second

a. Zero-order kinetics
b. First order kinetics

A

a. Zero-order kinetics

27
Q

Enzyme Level: _______ = Normal
Enzyme Level: ________ - Clinically significant

a. Low - Low
b. Low - High
c. High - Low
d. High - High

A

b. Low - High

28
Q

Most of the physiologic reaction occur in which pH range

A

pH = 7.0 to 8.0

29
Q

If the enzyme pH is too basic or too acid it could inactivate/denature enzyme. There is no exemption in this rule.

a. First statement is true, second statement is true.
b. First statement is false, second statement is true.
c. First statement is true, second statement is false.
d. First statement is false, second statement is false.

A

c. First statement is true, second statement is false.

Phosphatases are exempted in this rule.

30
Q

These enzymes could react in extremely high or low pH

A

Phosphatase

31
Q

assay temperature should be constant within what degree

A

± 0.1°C

32
Q

Optimum temperature for enzymatic activity

A

37°C

33
Q

Temperature range where protein denaturation starts and start of decreasing enzyme activity

A

40°C to 50°C

34
Q

Temperature range where proteins are inactivated

A

60°C to 65°C

35
Q

Temperature Coefficient(Q10) for every 10°C increase in temperature, there will be two-fold increase in enzyme activity. For storage, it should be at refrigerator temperature at 20°C or colder for maintaining enzymatic activity.

a. First statement is true, second statement is true.
b. First statement is false, second statement is true.
c. First statement is true, second statement is false.
d. First statement is false, second statement is false.

A

c. First statement is true, second statement is false.

For storage, it should be at freezer temperature at (-)20°C or colder.

*emphasis on the negative sign

36
Q

Why is multiple freezing and thawing of serum is not allowed?

A

It could damage or destroy the enzymes in the serum which results to false decrease of enzymes.

37
Q

What is the refrigerator temperature ideal for the storage of substrate and coenzyme?

A

2°C to 8°C

38
Q

What is the ideal storage temperature of serum sample wherein the target is LDH?

A

Room temperature

39
Q

What can falsely increase enzyme concentration?

A

Hemolyzed samples

40
Q

What could falsely decrease the enzyme concentration?

A

Milky specimens/ Lipemic samples

41
Q

Measurement of catalytic activity: (3)

A
  1. Dependent on enzyme concentration
  2. Always performed in zero-order kinetics
  3. Performed during the linear phase of reaction
42
Q

General methods of measuring enzymatic reaction: (2)

A
  1. Fixed-time (Two point) Assay
  2. Continuous monitoring
43
Q

General methods of measuring enzymatic reaction:

The reagents are combined, the reaction proceeds, the reaction is stopped and the amount of reaction is measured.

A

Fixed-time (Two point) Assay

44
Q

General methods of measuring enzymatic reaction:

Multiple measurements at specific time intervals or continuous measurement as absorbance changes. 30-60s interval; absorbance is noted.

A

Continuous monitoring

45
Q

An expression of the relationship between the velocity of the enzyme reaction and the substrate concentration

A

Michaelis-Menten Equation

46
Q

Calculation of Enzyme Activity:

The amount of enzyme that will catalyze the reaction of 1 μmol of substrate per minute.

A

IU (EC)

47
Q

Calculation of Enzyme Activity:

The amount of enzyme that will catalyze the reaction of 1 mol of substrate per second

A

Kat (SI)

48
Q

Enzyme Theories:

The shape of the key(substrate) must fit into the lock(enzyme)

A

Emil Fisher’s/ Lock and Key theory

49
Q

Enzyme Theories:

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

A

Kochland’s Induced Fit theory

cee cee 2 finals (5 decks)

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