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BIOCHEM > ENZYMOLOGY > Flashcards

ENZYMOLOGY Flashcards

1
Q

These are the several distinct forms of enzymes. Important in the diagnosis of specificity

A

ENZYME VARIANT

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2
Q

The multichained enzymes. Enzymes of similar activity typically appearing in specific tissue, organs and cell
organelles of organisms and the same species

A

ISOENZYMES

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3
Q

Specifically located in tissues. The site of a specific isoenzyme is found and restricted to only one tissue

A

ISOENZYMES

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4
Q

Lactate dehydrogenase subunits and bond

A

H and M subunits (polypeptide chains)

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4
Q

H4 – LD1

A

heart, RBC, and renal tissues

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4
Q

LD1

A

H4

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5
Q

H3M – LD2

A

heart, RBC and renal tissues

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6
Q

LD2

A

H3M

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7
Q

H2M2 – LD3

A

– lungs, lymphocytes, spleen, pancreas

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8
Q

LD3

A

H2M2

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9
Q

HM3 – LD4

A

liver, skeletal muscle

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10
Q

LD4

A

HM3

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11
Q

M4 – LD5

A

liver, skeletal muscle

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12
Q

LD5

A

M4

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13
Q

Response to activation and inactivation process : ACP (RBC)

A

not inhibited by 2% formaldehyde

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14
Q

Response to activation and inactivation process : ACP (prostate)

A

inhibited by 2% formaldehyde

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15
Q

Relative substrate specificity : ACP (RBC) is less sensitive to

A

α-naphthyl PO4 substrate

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16
Q

Same enzymatic activity, which are specie specific for different biological species

A

HETEROENZYMES

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17
Q
  • Genetically transmitted enzymes
  • Important in defining the biochemical characteristics of individuals
A

ALLOENZYMES

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18
Q
  • Present only in some selected individuals of the same species
  • Practical value in forensic medicine and genetics
A

ALLOENZYMES

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19
Q

Generally secreted by liver into the plasma. Enzymes exert function in plasma

A

Plasma Specific Enzymes

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20
Q

Enzymes that do not have specific function in plasma. The plasma lacks activators or coenzymes which are necessary for enzyme activity

A

Non-plasma specific enzymes

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21
Q

2 classes of Non-plasma specific enzymes

A
  • Enzyme of secretion
  • Enzymes associated with cellular metabolism
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22
Q

These are normally secreted enzymes like AMS

A

Enzyme of secretion

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23
Q

Enzymes secreted in plasma at a very high rate but are rapidly disposed off to normal excretory channels thus concentration in plasma is maintained at low and constant level

A

Enzyme of secretion

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24
Q

Enzymes that carry out their functions within the cells in which they are
formed. state examples

A

CK in heart and ACP in prostate gland

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25
Q

Enzymes based on distribution

A

A. Unilocular Enzymes
B. Bilocular enzyme

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26
Q

These are enzymes found only in the cell sap. Found only in one location

A

Unilocular Enzymes

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27
Q

These are enzymes that are found in the mitochondria and cell sap

A

Bilocular enzyme

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28
Q

formula of Enzyme Kinetics

A

E+S ——-> ES ——–> P+E

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29
Q

Enzyme Kinetics : E

A

= enzyme that represents a true catalyst
= not changed in the reaction

30
Q

Enzyme Kinetics : S

A

substrate upon which the enzyme acts

31
Q

Enzyme Kinetics : ES

A

the postulated enzyme – substrate complex

32
Q

Enzyme Kinetics : P

A

= the reacted substrate
= product that represents a changed molecular species of substrate

33
Q

this refers to the activation energy

34
Q

E + S = commonness and sameness between
enzyme and substrate

A

Molecular compatibility

35
Q

refers to the number of enzymes or substrates that can be reacted

A

Space availability

36
Q

refers to the particular enzyme catalyzing a specific substrate

A

Specificity

37
Q

Factors Affecting E and S Combination

A

A. Lock and Key
B. Induced Fit model

38
Q

refers to the active site being complementary in shape and size of the substrate

A

Lock and Key

39
Q

refers to the enzyme changing in shape during binding with
substrate. After binding, the shape of the enzyme complements with the binding
site

A

Induced Fit model

40
Q

a. direct relationship
b. An increase in the concentration of substrate results to an increase in the
rate of enzyme activity
c. No free binding site

A

Substrate concentration

41
Q

a. This refers to the condition when the enzymatic reaction is allowed to take
place
b. If the catalytic activity of an enzyme on the substrate is fast, it results to a
shorter enzymatic reaction time thereby the enzyme is freed and can act
again on the remaining substrate

42
Q

2 Phases of Enzyme Reaction

A

A. First Order Kinetics
B. Zero Order Kinetics

43
Q

Enzyme concentration is fixed and the substrate concentration is
varied

A

First Order Kinetics

44
Q

The rate of reaction is almost directly proportional to substrate
concentration at low values (lower substrate concentration than enzyme)

A

First Order Kinetics

45
Q

The rate of reaction dependent on substrate concentration and on enzyme concentration

A

First Order Kinetics

46
Q

The rate depends on the enzyme concentration and independent of substrate concentration

A

Zero Order Kinetics

47
Q

An increase in the enzyme concentration results to an increase in the catalytic activity of the enzyme

A

Zero Order Kinetics

48
Q

a. Direct relationship
b. An increase in the enzyme concentration result to an increase in the
catalytic activity of the enzyme

A

Enzyme Concentration

49
Q

the point at which the enzyme molecule is capable of catalyzing the substrate with regards to temperature
requirement

A

Optimum temperature

50
Q

optimum temperature

A

30-37C or 37-40C

51
Q

what temperature does enzyme undergoes inactivation and denaturation (range)

52
Q

refers to the increased reaxtion rate for every 10C increase
(rate of reaction is doubled)

53
Q

the point at which the reaction rate is greatest

A

optimum pH

54
Q

at pH __ many enzymes show maximum activity

55
Q

a. Required for full enzyme activity
b. These metal activators or inorganic entities help bind the substrate to the
active site by forming ionic bridges
c. These help substrate in orientation so it is attached to the protein at theproper point nd in the correct configuration

A

Activators

56
Q

Divalent Cations

A
  • Fe++
  • Ca++
  • Zn ++
57
Q

Monovalent anions

A

Cl-
Br-
NO3-

58
Q

Monovalent cations

59
Q

Substances that decrease the rate of enzyme reaction if these are
present in the reaction system

A

Inhibitors

60
Q

Binds to the active site, blocking the access of the substrate to the enzyme

A

competitive inhibition

61
Q

Inhibitor that
Binds elsewhere on the enzyme causing change in shape that interferes with substrate binding

A

non-competitive

62
Q

inhibitors bind with the ES completely; no
product formed

A

Uncompetitive

63
Q

When inhibitors are possibly removed from the system and enzyme is fully restored

A

Reversible inhibition

64
Q

Physical separation processes that remove inhibitors

A

a. Dialysis
b. Gel filtration

65
Q
  1. When inhibitors combine covalently with the enzyme
  2. Physical methods are ineffective in separating inhibitors
    from enzymes
A

Irreversible inhibition

66
Q

These must be present at the proper concentration for many enzyme reactions to take place

A

Coenzyme concentration

67
Q

These are essentially coenzymes that firmly bind with enzymes

A

Prosthetic Group

68
Q

It refers to the disruption of the structure of enzyme molecule (3-dimensional structure)
that leads to the loss of enzyme activity

A

Enzyme Denaturation

69
Q
  • Defined as the amount of enzyme which catalyzes the conversion of 1umol of substrate
    in 1 minute
  • Reported in IU/liter of sample
A

International Unit (IU)

69
Q
  • A unit of enzyme activity which converts 1 mol of substrate per second
  • Has not yet received universal acceptance
69
Q

the concentration of the product influences the rate of reaction

A

Feedback control

70
Q

an interaction takes place at a position other than the active site but affects the active site, either positively or negatively

A

Allosterism

71
Q

must be activated by removing a small
portion of the polypeptide chains.

A

proenzymes or zymogens

BIOCHEM (6 decks)

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