Enzymology Flashcards
0
Q
Catalyze the transfer of a chemical group other than hydrogen from one substrate to another
A
Transferase
1
Q
Catalyze the removal or addition of electrons
A
Oxidoreductases
2
Q
Catalyzes hydrolysis or splitting of a bond by addition of water
A
Hydrolases
3
Q
Catalyze removal of groups from substrate w/o hydrolysis. Product contains double bonds
A
Lyases
4
Q
Catalyze the intramolecular arrangement of the substrate
A
Isomerases
5
Q
Catalyze the joining of two substrate molecules coupled with breaking of the pyrophosphate bond in ATP or similar compound
A
Ligases
6
Q
Enzyme Nomenclature of Acid Phosphatase
A
E.C. 3.1.3.2
7
Q
Enzyme Nomenclature of Alkaline Phosphatase
A
E.C. 3.1.3.1
8
Q
Enzyme Nomenclature of Amylase
A
E.C. 3.2.1.1
9
Q
Enzyme Nomenclature of Alanine Aminotransferase
A
E.C.2.6.1.2
10
Q
Enzyme Nomenclature of Aspartate Aminotransferase
A
E.C.2.6.1.1
11
Q
Enzyme Nomenclature of Aldolases
A
E.C.4.1.2.13
12
Q
Enzyme Nomenclature of Angiotensin Converting Enzyme
A
E.C. 3.4.15.1
13
Q
Enzyme Nomenclature of Creatine Kinase
A
E.C. 2.7.3.2
14
Q
E.C. 3.1.1.7
A
Enzyme Nomenclature of True/Acetyl Cholinesterase
15
Q
Enzyme Nomenclature of Pseudocholinesterase
A
E.C. 3.1.1.8
16
Q
Enzyme Nomenclature of Gamma Glutamly Transferase
A
E.C. 2.3.2.2
17
Q
Enzyme Nomenclature of G-6-PD
A
E.C. 1.1.1.49
18
Q
Enzyme Nomenclature if Lipase
A
E.C. 3.1.1.3
19
Q
Enzyme Nomenclature of Lactic Dehydrogenase
A
E.C. 1.1.1.27
20
Q
Enzyme Nomenclature of 5’Nucleotidase
A
E.C. 3.1.3.5
21
Q
Higher the enzyme the higher the reaction
A
Enzyme Conc.
22
Q
Amount of enzyme exceeding the amount of substance
A
Substrate Conc.
23
Q
Needed in the enzyme in order to have its activity
A
Cofactors
24
Organic compound
Increase the velocity of an enzymatic reaction
NAD
Coenzymes
25
Coenzymes if bound tightly
Prosthetic group
26
Addition if apoenzyme
Holoenzymes
27
Inorganic ions
Alters spatial configuration of the enzyme
Ca, Zn, Cl, Mg
Activators
28
Inorganic ion attached to a molecule
Metallonenzyme
29
Physically bind to the active site of an enzyme
Competitive inhibitor
30
Both the substrate and inhibitor compete for the same active site of the enzyme
Competitive inhibitor
31
The effect of the Competitive inhibitor can be counterattack by what to bind the enzyme?
Adding excess substrate
32
Binds an enzyme at a place other than the active site
Non-Competitive inhibitor
33
Inhibitor binds the enzyme independently from the substrate
Non-Competitive inhibitor
34
Substrate and inhibitor may bind an enzyme simultaneously
Non-Competitive inhibitor
35
The inhibitor binds to the enzyme-substrate complex
Uncompetitive inhibitor
36
Increasing substrate concentration, increases inhibition
Uncompetitive inhibitor
37
Enzymes having the same catalytic reactions but slightly different molecular structures
Isoenzymes
38
Temp where enzymes are active
25, 30, 37
39
Temp where enzymes are denaturated
40-50
40
Temp where enzymes are inactived
60-65
41
For every 10'C inc in temp, there will be a two-fold increase in enzyme activity
Temperature Coefficient Q10
42
Most physiologic reaction occur
pH range of 7-8
43
Storage of preservation for longer period of time
20 degrees C
44
Storage for temp ideal for substrate and coenzymes
2-8 degrees C
45
Ideal storage for LDH (LD4 and LD5)
Room temp
46
Substrate interacts with particular charge amino acid residues
Active site
47
Cavity other than the active site; may bind regulator molecules
Allosteric site
48
The shape of the key must fit into the lock (substrate is specific to one enzyme)
Emil Fisher's/Lock and Key Theory
49
Based on the substrate binding to the active site of the enzyme
Kochland's/Induced Fit Theory
50
Combines with only one substrate and catalyzes only one reaction
Absolute specificity
51
Enzymes combine with all the substrate in a chemical group
Group specificity
52
Enzymes reacting with specific chemical bonds
Bonds specificity
53
Reaction rate depends only enzyme conc.
Zero-order reaction
54
Reaction rate is directly proportional to substrate conc.
First-order reaction
55
The reactants are combined; the reaction proceeds for a designated time
The reaction is stopped and measurement is made
Fixed-Time
56
Multiple measurements of absorbance changed are made during the reaction; more adventurous than fixed-time
Continuous monitoring/Kinetic assay
57
Predominant physiologic functions occurs in muscle cells.
Creatine Kinase
58
Catalyzes the transfer of a phosphate group bet creatine phosphate and adenosine diphosphate
Creatine Kinase
59
Sensitive indicator of AMI and muscular dystrophy-Duchenne type (50-100x)
Creatine Kinase
60
Highest tissue source of CK
Heart, skeletal, smooth muscle, brain tissue
61
Smallest tissue source found in the CK
Bladder, placenta, uterus, kidney, GiT, thyroid, lungs, prostate, spleen, liver, pancreas
62
Size of CK
Dimeric molecules
63
Composed of two different monomers
M and B
64
Major isoenzyme in the serum of the healthy people
CK-MM( muscle type) / CK3
65
Major activity of CK-MM are found where?
In the heart
66
Undetectable/trace
| Hybrid type
CK-MB
67
Migrates in the middle of CKMM and CKMB
Macro CK
68
Migrates cathodal to CK MM; Indicator of severe illness
Mitochondrial CK
69
Methods used in Creatine Kinase: it requires a pH of 9.0-10.0; 340nm
Tanzer-Gilbarg Assay (forward/direct method)
70
Methods used in Creatine Kinase: most commonly used method; faster reaction; pH 6.8; 340 nm
Oliver-Rosalki(reverse/indirect method)
71
Specimen considerations: added to the reverse method to inhibit AK which may be present in the serum from hemolysis
Adenosine monophosphate (AMP)
72
Specimen considerations: serves as buffer; component also of CK rgt
Imidazole
73
Specimen considerations: partially restore lost activity of CK
Cleland's reagent and gluthatione
74
Specimen considerations: added to CK rgt to activate the enzyme
N-acetylcysteine
75
Specimen considerations for Creatine Kinase:
Urate and cysteine are potent inhibitors
Liver cells and RBC do not contain CK
CK is light and pH sensitive; it is also lost with excessive storage
76
Catalyzes the interconversion of lactic and pyruvic acids
Lactate Dehydrogenase
77
Molecular form of Lactate Dehydrogenase
Tetrametric molecule
78
Highest tissue source of Lactate Dehydrogenase
Heart, liver, skeletal muscle, kidney, erythrocytes
79
Lesser amount of tissue source in Lactate Dehydrogenase
Lung, smooth muscle, brain
80
Isoenzymes of Lactate Dehydrogenase: Heart and RBC (higher than LD2), kidney
LD1
81
Isoenzymes of Lactate Dehydrogenase: same as LD1, major isoenzymes
LD2
82
Isoenzymes of Lactate Dehydrogenase: in lungs, pancreas, spleen
LD3
83
Isoenzymes of Lactate Dehydrogenase: in skeletal muscle, liver, intestine
LD4
84
Isoenzymes of Lactate Dehydrogenase: significant in hepatic disorder; liver, skeletal(higher than Ld4), intestine
LD5
85
Isoenzymes of Lactate Dehydrogenase: arteriosclerotic cardiovascular failure
LD6
86
Onset for AMI:
12-24 hrs
87
Peak for AMI
48-72 hrs
88
Remain elevated for AMI
10 days
89
Highest level are seen where in Lactate Dehyrdogenase
Pernicious anemia and hemolytic disorders
90
It has a 10 fold increased in Lactate Dehydrogenase
Hepatic Carcinoma and toxic hepatitis
91
Transudate from exudates
Pleural fluids
92
Specimen consideration for Lactate Dehydrogenase: substrate; high affinity in H subunits
Alpha-hydroxybutyrate
93
Methods for Lactate Dehydrogenase: most commonly used method
pH 8.8
Preferred for LD1
Wacker Method (forward/direct reaction)
94
Methods for Lactate Dehydrogenase:
2x faster as the forward reaction
pH 7.2
Preferred for LD5
Wrobleuski La Due (reverse/indirect reaction)
