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CC 2 LEC > Enzymology > Flashcards

Enzymology Flashcards

1
Q

Proteins produced by living cells that hasten chemical reactions in organic matter.

A

Enzymes

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2
Q

Measured in terms of their activity and not in terms of their absolute value

A

Enzymes

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3
Q

T or F: The higher the enzyme concentration, the faster the reaction.

A

True (more enzyme is present to bind the substrate)

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4
Q

10 Factors affecting enzyme reaction.

A
  1. Enzyme concentration
  2. Substrate concentration
  3. Cofactors
  4. Inhibitors
  5. Isoenzymes
  6. Temperature
  7. Hydrogen ion concentration or pH
  8. Storage
  9. Hemolysis
  10. Lactescense or milky specimen
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5
Q

Example of activators. (CCMPZ)

A
  • calcium
  • chloride
  • magnesium
  • potassium
  • zinc
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6
Q

Examples of metalloenzymes. (CC)

A
  • catalase
  • cytochrome oxidase
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7
Q

3 types of inhibitor.

A
  • competitive inhibitor
  • non-competitive inhibitor
  • uncompetitive inhibitor
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8
Q

Physically binds to the active site of an enzyme

A

Competitive inhibitor

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9
Q

Does not compete with the substrate but look for areas other than the active site.

A

Non-competitive inhibitor

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10
Q

Binds to the enzyme-substrate complex

A

Uncompetitive inhibitor

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11
Q

Enzymes are active on what temperature?

A

25C, 30C, 32C

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12
Q

Optimum temp. for enzymatic activity

A

37C

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13
Q

Rate of denaturation is usually significant at what temp.?

A

40 - 50C

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14
Q

Temp. that may result in activation of enzymes

A

60-65C

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15
Q

Most physiologic enzyme reaction occur in what pH?

A

range 7-8 pH

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16
Q

Ideal temp. for preservation of enzyme

A

-20 deg. C

17
Q

Ideal storage temp. for substrate and coenzymes

A

2 - 8 degree C

18
Q

Ideal temp. storage for LDH (LD4 and LD5)

A

22Cto room temp.

19
Q

Hemolysis decreases enzyme concentration. Lactescense/milky spx. increases enzyme concentration.

A

Both statement is false.
Hemolysis - increases
Lactescence - decreases

20
Q

Catalyze the removal or addition of electrons (redox reaction)

A

Oxidoreductases
- CO, LDH, MDH, ICD, G-6-PD

21
Q

Catalyze the transfer of a chemical group other than hydrogen from one substrate to another.

A

Transferases
- CK, AST, ALT, OCT

22
Q

Catalyzehydrolysis or splitting of a bond by the addition of water (hydrolytic reactions)

A

Hydrolases
- Esterases: ACP, ALP, CHS, LPS
- Peptidases: Trypsin, Pepsin, LAP
- Glycosidase: AMS, Galactosidases

23
Q

Catalyze removal of groups from substrates without hydrolysis. The product contains double bonds.

A

Lyases
- Glutamate decarboxylase, Pyruvate decarboxylase, Tryptophan decarboxylase and Aldolase

24
Q

Catalyze the intramolecular arrangement of the substrate compound

A

Isomerases
- Glucose phosphate isomerase and Ribose phosphate isomerase

25
Q

Catalyze the joining of two substrate molecules, coupled with breaking of the pyrophosphate bonding ATP or similar compound.

A

Ligases
- Synthase

26
Q

Based on the premise that the shape of the key (substrate) must fit into the lock (enzyme)

A

Emil Fisher’s/Lock and Key theory

27
Q

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

A

Kochland’s/Induced fit theory

28
Q

An enzymes combines with only one substrate and catalyzes only one reaction is known as ________

A

Absolute specificity

29
Q

Enzymes combined with all the substrates in a chemical group is called _______

A

Group specificity

30
Q

Enzymes reacting with specific chemical bonds is known as _________

A

bond specificity

31
Q

1 micromole of substrate/minute

A

International Unit (IU or U)

32
Q

1 mole of substrate/second

A

Katal unit (KU)

33
Q

Enzymes are measured in terms of:

A
  1. Change in substrate concentration
  2. Change in product concentration
  3. Change in coenzyme concentration
34
Q

The reaction rate depends only on enzyme concentration.

A

Zero-order reaction

35
Q

the reaction rate is directly proportional to substrate concentration

A

the reaction rate is directly proportional to substrate concentration

36
Q

It is a nonspecific enzyme capable of reacting with many different substrates.

A

Alkaline phosphate

37
Q

functions to liberate inorganic phosphate from an organic phosphate ester with the concomitant production of an alcohol.

A

Alkaline phosphate

38
Q

Major tissue sources of Alkaline phosphate (LBPI)

A

Liver, Bone, Placenta, Intestinal

39
Q

Reference value of Alkaline Phosphate

A

30-90 U/L

CC 2 LEC (1 decks)

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