Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

CC2 LECTURE > Module 1: Enzymology > Flashcards

Module 1: Enzymology Flashcards

1
Q

These are proteins produced by living cells that hastens chemical reactions in organic matter

A

Enzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Enzymes are measured in terms of _____ and not in terms of their absolute values

A

Activity

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Enzymes are _____ molecules and they are normally confined within cells unless increased membrane permeability _____ them to enter the blood

A

Large molecules; allows

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Enzymes appear in the serum after ______, _____, or ______

A

Cellular injury, degradation of cells or from storage areas

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

(T/F)
Abnormal large amounts of enzymes in serum
are used clinically as evidence of organ damage

A

True

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

T/F
Each enzyme catalyzes a single reaction or a limited number of chemical reactions, and it is specific for a substrate that it converts to a defined
product

A

true

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Factors affecting enzymatic reactions

A

Enzyme concentration
Substrate concentration
Cofactors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

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

A

Enzyme concentration

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

With the amount of enzyme exceeding the amount of substrate, the reaction rate steadily increases as more substrate is added

A

Substrate concentration

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

However, when the substrate concentration reaches a maximal value, higher concentration of substrate no longer result in increased rate of reaction (________)

A

Saturation kinetics

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Nonprotein entities that must bind to particular enzymes before a reaction occurs

A

Cofactors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Is an organic compound (second substrate)

A

Coenzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Coenzymes
(T/F)
Increasing its concentration will increase the
velocity of an enzymatic reaction

A

true

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

It is essential to achieve absolute enzymatic activity

A

Coenzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Examples of Coenzymes

A

NAD
NADP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Are inorganic ions which alters the spatial configuration of the enzyme for proper substrate
binding

A

Activators

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Examples of Activators

A

Calcium
Zinc
Chloride
Magnesium
Potassium

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Are inorganic ions attached to a molecule

A

Metalloenzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Examples of Metalloenzymes

A

Catalase
Cytochrome oxidase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Enzymatic reactions may not progress if an inhibitor interferes with the reaction

A

Inhibitors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

Physically binds to the active site of an enzyme

A

Competitive inhibitors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

It does not compete with the substrate but look for areas other than the active site

A

Non-competitive inhibitors

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

The inhibitor binds to the enzyme-substrate (ES) complex

A

Uncompetitive inhibitor

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

These are enzymes (polypeptide chains) having the same catalytic reactions but slightly different molecular structures – various forms occur because of differences in the amino acid sequence of enzymes

A

Isoenzymes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Enzymes are active at ____, ____, and ____

A

25°C, 30°C, and 37°C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

____ is the optimum temperature for enzymatic
activity

A

37°C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

(T/F)
Increasing temperature usually increases the rate of
a chemical reaction by increasing the movement of
molecules

A

true

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

The rate of denaturation increases as the
temperature increases, and is usually significant at
____ to ____

A

40°C to 50°C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

______ may result to inactivation of enzymes

A

60-65°C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

means for every 10°C increase in temperature, there will be a two-fold increase in enzyme activity

A

Temperature Coefficient (Q10)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Hydrogem ion concentration/pH

Most physiologic reactions occur in the pH range of __ to __

A

7 to 8

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

(T/F)
Extreme pH level may denature an enzyme or influence its ionic state resulting in structural change or change in the charge of amino acid residue in the active site

A

true

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

render enzymes reversibly inactive

A

Low temperature (refrigeration/freezing)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

tends to denature proteins and should be avoided

A

Repeated freezing and thawing

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

preservation for longer period of time (enzymes)

A

-20°C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

ideal storage temperature for substrate and coenzymes

A

2° to 8°C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

ideal for storage of LDH (LD4 and LD5)

A

Room temperature

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

Mostly increases enzyme concentration

A

Hemolysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

Decreases enzyme concentration

A

Lactescence or Milky Specimen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

To standardize enzyme nomenclature, the _______ adapted a classification system in 1961, and revised the standards in 1972 and 1978

A

Enzyme Commission (EC)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

Enzymes are classified according to their ________, indicating a substrate and class of reaction catalyzed, and are designated by individual identification numbers

A

Biochemical functions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

The first digit, places the enzyme in its _______

A

classifications (six classifications)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

The second and third digits, represents the _______ to which the enzyme is assigned

A

subclass

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

The final and fourth number/s, is a _______ that is specific to each enzyme in a subclass

A

serial number

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

E.C. 3.1.3.2

A

Acid Phosphatase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

E.C. 3.1.3.1

A

Alkaline Phosphatase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

E.C. 3.2.1.1

A

Amylase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

E.C. 2.6.1.2

A

Alanine Aminotransferase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
49
Q

E.C. 2.6.1.1

A

Aspartate Aminotransferase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
50
Q

E.C. 4.1.2.13

A

Aldolase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
51
Q

E.C. 3.4.15.1

A

Angiotensin Converting Enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
52
Q

E.C. 2.7.3.2

A

Creatine Kinase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
53
Q

E.C. 3.1.1.7

A

True/Acetyl Cholinesterase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
54
Q

E.C. 3.1.1.8

A

Pseudocholinesterase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
55
Q

E.C. 2.3.2.2

A

Gamma Glutamyl Transferase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
56
Q

E.C. 1.1.1.49

A

G-6-PD

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
57
Q

E.C. 3.1.1.3

A

Lipase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
58
Q

E.C. 1.1.1.27

A

Lactic Dehydrogenase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
59
Q

E.C. 3.1.3.5

A

5’ Nucleotidase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
60
Q

Catalyze the removal or addition of electrons (redox reaction)

A

Oxidoreductases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
61
Q

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

A

Transferases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
62
Q

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

A

Hydrolases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
63
Q

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

A

Lyases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
64
Q

Catalyzes the intramolecular arrangement of the substrate compound

A

Isomerases

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
65
Q

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

A

Ligases

66
Q

is water-free cavity, where the
substrate interacts with particular charged amino acid residues; is a 3-dimensional protein structure

A

Active site

67
Q

is a cavity other than the active site; may bind regulator molecules

A

Allosteric site

68
Q

When bound tightly to the enzyme, the coenzyme is called a _______

A

prosthetic group

69
Q

Apoenzyme (enzyme portion) and coenzyme forms a complete and active system known as _______

A

holoenzyme

70
Q

Digestive enzymes in its inactive form originally secreted from the organ of production is called a ______ or ______

A

proenzyme or zymogen

71
Q

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

A

Emil Fisher’s Theory / Lock and Key Theory

72
Q

Is based on the substrate binding to the active site of the enzyme

A

Kochland’s Theory / Induced Fit Theory

73
Q

A chemical reaction may occur spontaneously if the free energy or available kinetic energy is higher for the substrate than the product

A

Enzyme kinetics

74
Q

(T/F)
An enzyme combines with only one substrate and catalyzes only one reaction (absolute specificity)

A

true

75
Q

the reaction rate depends only on enzyme concentration

A

Zero-order reaction

76
Q

the reaction rate is directly proportional to substrate concentration

A

First-order reaction

77
Q

the reactants are combined; the
reaction proceeds for a designated time; the
reaction is stopped and measurement is made

A

fixed-time

78
Q

multiple measurements of changed in absorbance are made during the reaction; it is
preferred than fixed-time

A

Continuous monitoring/kinetic assay

79
Q

1 micromole of substrate/minute

A

International Unit (IU or U)

80
Q

1 mole of substrate/second

A

Katal Unit (KU)

81
Q

The units used to report enzyme levels are _______

A

activity units

82
Q

(T/F)
Most enzymes are measured by monitoring the rate of absorbance change (kinetic assay) at 340nm as NADH is reduced or consumed, and it allows direct reporting either by IU or KU

A

true

83
Q

In nonkinetic assay, absorbance is made at ________

A

10-second intervals for 100 seconds

84
Q

Is a nonspecific enzyme capable of reacting with many different substrates

A

alkaline phosphatase

85
Q

other name of ALP

A

Alkaline Orthophosphoric Monoester Phosphohydrolase

86
Q

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

A

ALP

87
Q

In healthy sera, alkaline phosphatase (ALP) levels are derived from ____ and ____

A

liver
bone (osteoblasts)

88
Q

__ or __ blood group increases intestinal ALP after consumption of a fatty meal

A

B or O

89
Q

major tissue sources of ALP

A

liver, bone, placenta, and intestinal

90
Q

RV for ALP

A

30-20 U/L

91
Q

major isoenzymes of ALP

A

liver ALP, bone ALP, placental
ALP, and intestinal ALP

92
Q

carcinoplacental ALP

A

regan ALP, nagao ALP

93
Q

Is found in lung, breast, ovarian, and gynecological cancers; bone ALP co-migrator; most heat stable ALP (65°C for 30 minutes); inhibited by phenylalanine reagent

A

regan ALP

94
Q

Found in adenocarcinoma of the pancreas and bile duct, pleural cancer; variant of regan ALP; inhibited by L-leucine and phenylalanine

A

nagao ALP

95
Q

ELECTROPHORESIS
_____ and _____ ALPs are the most anodal isoenzymes

______ ALP is the least anodal

A

liver and bone

intestinal

96
Q

(T/F)
High-resolution electrophoresis using polyacrylamide gel and isoelectric focusing are capable of resolving multiple bands of ALP

A

true

97
Q

It is performed at 56°C for 10-15 minutes

A

heat fractionation/stability test

98
Q

HF/Stability test
______ ALP is the most heat stable; _____ ALP is
the most heat labile

A

placental
bone

99
Q

Decreasing order of ALP heat stability:

A

placental,
intestinal, liver, and bone

100
Q

This method uses different concentrations of phenylalanine, synthetic urea, and levamisole solutions

A

chemical inhibition test

101
Q

Placental and intestinal ALPs are inhibited by ________ and ______ inhibits bone ALP

A

phenylalanine reagent
3M urea

102
Q

______ reagent inhibits liver and bone ALP

A

Levamisole

103
Q

Is considered as the most specific method; IFCC recommended method

A

Bowers and McComb (Szasz Modification)

104
Q

It is a continuous-monitoring technique which requires a pH environment of 10.15 and should be read at 405nm

A

Bowers and McComb

105
Q

It catalyzes the same reaction by ALP, except that it is active at pH 5.0

A

acid phosphatase

106
Q

other name of ACP

A

Acid Orthophosphoric Monoester Phosphohydrolase

107
Q

tissue sources of ACP

A

prostate (major source), RBCs, platelets, liver, and bone

108
Q

RV for ACP

A

Male = 2.5-11.7 U/L (Total ACP), 0-3.5 ng/mL (Prostatic ACP)

109
Q

For detection of prostatic adenocarcinoma

A

ACP

110
Q

It is also useful in forensic clinical chemistry, in the
investigation of rape cases – vaginal washings are examined for seminal fluid-ACP activity, which can persists for up to 4 days

A

ACP

111
Q

Is involved in the transfer of an amino group between aspartate and 𝛼-keto acids with the formation of oxaloacetate and glutamate

A

Aspartate Aminotransferase (AST)

112
Q

AST
the ________ is the predominant form in serum

A

cytoplasmic isoenzyme

113
Q

major tissue sources of AST

A

cardiac tissue, liver, and skeletal muscle

114
Q

other sources of AST

A

kidney, pancreas, and RBC

115
Q

RV for AST

A

5-37 U/L

116
Q
  • pH 7.5; 340 nm
  • It uses malate dehydrogenase (MD) and monitors
    the change in absorbance at 340 nm
A

karmen method

117
Q

It has enzymatic activity similar to AST

A

Alanine Aminotransferase (ALT)

118
Q

It catalyzes the transfer of an amino group from alanine to 𝛼-ketoglutarate with the formation of glutamate and pyruvate

A

ALT

119
Q

The highest concentration is in the liver; more liver-specific than AST

A

ALT

120
Q

major tissue source of ALT

A

liver

121
Q

other soruces of ALT

A

kidney, pancreas, RBC, heart,
skeletal muscle, and lungs

122
Q

RV for ALT

A

6-37 U/L

123
Q

Aminotransferases are present in ______, _____, _____, and ______

A

human plasma, bile, CSF, and saliva

124
Q

Aminotransferases require ________ (vitamin B6) as coenzyme (prosthetic group)

A

pyridoxal phosphate

125
Q

Using pH 7.5; reading at 340 nm

A

couple enzymatic reaction

126
Q

Is an enzyme that catalyzes the interconversion of lactic and pyruvic acids

A

Lactate Dehydrogenase

127
Q

Is a zinc-containing enzyme that is part of the glycolytic pathway and is found in virtually all cells in the body

A

lactate dehydrogenase

128
Q

tissue sources of LDH

A

heart, RBCs, kidneys (LD-1 & LD-2); lungs, pancreas, spleen (LD-3); skeletal muscles, liver, intestine (LD-4 & LD-5)

129
Q

RV for LDH

A

100-225 U/L (forward reaction), 80-280 U/L (reverse reaction)

130
Q
  • Reaction is at pH 8.8
  • Is the most commonly used method because it produces a positive rate (NADH) and not affected by product inhibition
A

wacker method (forward/direct reaction)

131
Q
  • Reaction is at pH 7.2
    ● It is about 2x faster as the forward reaction
    ● It is the preferred method for dry slide technology
    ● It uses a less costly cofactor and it has a smaller
    specimen volume requirement
A

wrobleuski la due (reverse/indirect reaction)

132
Q

other methods for LDH

A

wrobleuski cabaud
berger broida

133
Q

It catalyzes the transfer of a phosphate group between creatine phosphate and adenosine diphosphate

A

creatine kinase

134
Q

other name for CK

A

ATP-CREATINE-N-PHOSPHOTRANSFERASE

135
Q
  • It is involved in the storage of high-energy creatine PO4 in the muscles
    ● It is a dimeric molecule with small molecular size, composed of a pair of two different monomers called M and B
    ● It is found in small amounts throughout the body, but it is found in high concentrations only in muscle and brain, although CK from brain virtually never crosses the blood-brain barrier to reach plasma
A

CK

136
Q

major tissue sources of CK

A

brain tissue, smooth and skeletal muscle, and cardiac muscles

137
Q

RV for CK

A

Male = 15-160 U/L, Female = 15-130 U/L, CK-MB = <6% of total CK

138
Q

isoenzymes for CK

A

CK-BB (brain type), CK-MB (hybrid type), CK-MM (muscle type)

139
Q

methods for CK

A

tanzer-gilbarg assay
oliver-rosalki

140
Q

most commonly used method; faster reaction for CK

A

oliver-rosalki

141
Q

Is an expression of the percentage of the total CK that is attributed to CK-MB. This is commonly to know possible release of CK-MB from noncardiac tissues when total CK is very high

A

CK relative index (CKI)

142
Q

It catalyzes the breakdown of starch and glycogen – an important enzyme in the physiologic digestion of starch

A

amylase

143
Q

It is the smallest enzyme in size (with a MW of 50,000 to 55,000 daltons) – normally filtered by the renal glomerulus and also appears in the urine

A

amylase

144
Q

major tissue sources of amylase

A

acinar cells of the pancreas
and the salivary glands

145
Q

other tissue sources of amylase

A

adipose tissue, fallopian
tubes, small intestine and skeletal muscles

146
Q

RV for amylase

A

60-180 SU/dL (somogyi units) &
95-290 U/L

147
Q
  • It is the classic reference method expressed in Somogyi units
    ● It measures the amount of reducing sugars produced by the hydrolysis of starch by the usual glucose methods
A

saccharogenic

148
Q

It measures amylase activity by following the decreases in substrate concentration (degradation of starch)

A

amyloclastic

149
Q

It measures amylase activity by the increase in color intensity of the soluble dye-substrate solution produced in the reaction

A

chromogenic

150
Q

It measures amylase activity by a continuous-monitoring technique

A

coupled-enzyme

151
Q

Is an enzyme that hydrolyzes the ester linkages of fats to produce alcohol and fatty acid

A

lipase

152
Q

Major tissue source: Pancreas
Reference value: 0-1.0 U/mL

A

lipase

153
Q

hydrolysis of olive oil after incubation for 24 hours at 37°C and titration of fatty acids using NaOH

A

cherry crandal

154
Q

Most commonly used method; does not use 50%
olive oil

A

peroxidase coupling

155
Q

Is a phosphoric monoester hydrolase; predominantly secreted from the liver

A

5’ nucleotidase

156
Q

It catalyzes the transfer of glutamyl groups between peptides or amino acids through linkage at a gammy carboxyl group

A

GGT

157
Q

It is secreted by the liver – it reflects synthetic function rather than hepatocyte injury

A

pseudocholinesterase

158
Q

Is also known as “peptidyldipeptidase A” or “kininase il”; a hydrolase enzyme

A

angiotensin-converting enzyme

159
Q
  • Is a copper-carrying protein and also an enzyme
    ● Is a marker for Wilson’s disease (hepatolenticular
    disease)
A

ceruloplasmin

160
Q

Is a marker for hepatobiliary disease

A

ornithine carbamoyl transferase

161
Q

It functions to maintain NADPH in the reduced form in the erythrocytes

A

G6PD

CC2 LECTURE (1 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions