Enzymes

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1
Terminology for proteins that catalyze biochemical reactions without altering the equilibrium point
Enzymes
2
Identify the characteristic of enzymes regarding their consumption in a reaction
not consumed or altered
3
Specify the enzyme class that catalyzes oxidation-reduction reactions
Oxidoreductases
4
List two examples of oxidoreductase enzymes
lactate dehydrogenase and G6PD
5
Specify the enzyme class that catalyzes the transfer of a group other than hydrogen
Transferases
6
List four examples of transferase enzymes
aspartate transaminase, alanine transaminase, creatine kinase, and gamma-glutamyl transferase
7
Specify the enzyme class that catalyzes the hydrolysis of ether and ester bonds
Hydrolases
8
List four examples of hydrolase enzymes
alkaline phosphatase, acid phosphatase, amylase, and cholinesterase
9
Specify the enzyme class that catalyzes the removal of groups without hydrolysis
Lyases
10
Specify the enzyme class that catalyzes the interconversion of geometric or optical isomers
Isomerases
11
Specify the enzyme class that catalyzes the joining of two substrate molecules
Ligases
12
Describe the relationship of reaction rate to substrate concentration in First order kinetics
directly proportional
13
Define the point at which the reaction rate no longer responds to increased substrate concentration
Zero order
14
State the formula for the catalytic mechanism
E + S = ES = E + P
15
Identify the constant that expresses the relationship between reaction velocity and substrate concentration
Michaelis-Menten constant (Km)
16
Define the plot that expresses Km as a straight line where Vmax is the reciprocal of the y-intercept
Lineweaver-Burk plot
17
In a Lineweaver-Burk plot, identify what the negative reciprocal of the x-intercept represents
Km
18
Identify the measurement type performed after a reaction proceeds for a designated length of time and is stopped
Endpoint
19
Identify the measurement type involving multiple measurements of absorbance change at specific time intervals
Kinetic
20
Identify the enzyme classification of GGT (Gamma-glutamyl transferase)
Transferases (Group 2)
21
Enumerate the major enzyme groups and their characteristic endings or examples
Oxidoreductase (dehydrogenases, oxidases); Transferase (kinases, transaminases); Hydrolases (amylase, ACP, ALP, lipase); Lyases (decarboxylases, aldolase); Isomerase (isomerases); Ligase (synthetases)
22
Identify the chemical action of Oxidoreductases
Redox - Dehydrogenase
23
Identify the chemical action of Transferases
Transfer of group, except water, from one substrate to another
24
Identify the chemical action of Hydrolases
Breakage of bond with hydrolysis (addition of water)
25
Enumerate the specific types of Hydrolase enzymes
Esterases (Cholinesterase, ACP, Lipase, ALP); Peptidases (Pepsin, trypsin, LAP); Glycosidases (Amylase, galactosidases)
26
Identify the chemical action of Lyases
Removal of groups without water
27
Identify the chemical action of Isomerases
Intermolecular arrangement
28
Identify the chemical action of Ligases
Joining of 2 substrates
29
Identify the physiological effect of high concentrations of Hgb and Bilirubin on ACP determination
False decrease (interference)
30
Enumerate the conditions associated with an LD-flipped pattern (LD1 > LD2)
MI, Megaloblastic anemia, Hemolysis, Hemolytic Disorders, Renal Infarction, Renal carcinoma
31
Identify the most specific substrate for ACP (Acid Phosphatase)
Thymolphthalein monophosphate
32
Identify the reference method for ACP
Thymolphthalein monophosphate
33
Enumerate the conditions characterized by a pronounced elevation of AST (5 or more times normal)
MI, Acute pancreatitis / pancreatic insufficiency, Acute hepatitis, Circulatory collapse (shock), Infectious mononucleosis
34
Enumerate the conditions characterized by a moderate elevation of AST (3 to 5 times normal)
Biliary tract obstruction (Cholelithiasis), Cardiac arrhythmias, Congestive heart failure, Metastatic or primary tumor in liver, Muscular dystrophy (Duchenne)
35
Enumerate the conditions characterized by a slight elevation of AST (up to 3 times normal)
Pericarditis, Cirrhosis, Pulmonary infarction, Delirium tremens, Cerebrovascular accident (stroke)
36
Enumerate all conditions where ALP is increased five-fold (5x), following the BOBOH acronym
Biliary Duct Obstruction, Osteitis deformans (Paget's disease), Biliary cirrhosis, Osteosarcoma (Osteogenic sarcoma), Hyperparathyroidism
37
Identify the specific salivary gland enzyme also known as Ptyalin
Amylase
38
Enumerate the major tissue sources and the size characteristic of serum Amylase
ACINAR cells of the PANCREAS and SALIVARY glands; SMALLEST enzyme
39
Identify the primary and secondary digestion sites for Amylase
Primary: mouth (ptyalin); Secondary: small intestine (amylopsin)
40
Enumerate the conditions where total LDH is markedly increased to its highest levels
Megaloblastic anemia and Pernicious anemia
41
Identify the only enzyme significant for being measured in decreased amounts
Pseudocholinesterase
42
Enumerate all conditions where Pseudocholinesterase is decreased
Hepatic Disease, Organophosphate poisoning (insecticide/pesticide), Genetic variants, Suxamethonium sensitivity (anesthesia)
43
Liver specific enzymes include
ALT and AST
44
Enzyme localized in the pancreas and salivary gland
Amylase
45
Pancreas specific enzyme
Lipase
46
Enzymes found in the liver, heart, and skeletal muscles
AST
47
Enzymes found in the heart, skeletal muscles, and brain
CK
48
Enzymes found in the liver, bone, and kidney
ALP
49
The total LDH is known for low specificity and is found in
all tissues
50
Wacker and Wroblewski and are methods associated with
LDH
51
LD isoenzyme found in the lung, spleen, pancreas, thyroid, and adrenal lymph nodes
LD3
52
LD isoenzymes associated with liver and skeletal muscles
LD4 and LD5
53
The most labile LD isoenzymes are
LD5 and LD4
54
Specific name for LD6
Alcohol Dehydrogenase
55
The endpoint method for ALT and AST is
Reitman-Frankel
56
The kinetic method for ALT and AST is
Karmen
57
The common products of Reitman-Frankel and Karmen methods are
oxaloacetate and pyruvate
58
Saccharogenic, Amyloclastic (starch), Colorimetric, and Coupled enzymatic are methods for
Amylase
59
Amylase is defined as the function of a reduced
sugar or alcohol
60
The first enzyme to increase in Myocardial Infarction (MI)
CK-MB
61
The first protein to increase in Myocardial Infarction (MI)
MYOGLOBIN
62
The most specific marker for Myocardial Infarction (MI)
TROPONIN
63
The last enzyme to increase in Myocardial Infarction (MI)
LDH
64
CK-MB rise time, peak time, and normalization time
increase 4-8 hours, peak 12-24hrs, normalizes 48-72hrs
65
Condition associated with Hyperkalemia, Dehydration, Intravascular hemolysis (DIHA), Hypoaldosteronism, and Acidosis
Cardiac Arrhythmia
66
Organs/cells that act as producers of Acid Phosphatase (ACP)
Prostate gland, erythrocytes, platelets, spleen, liver, kidney, bones (PEPSLK-B)
67
Level of ACP in Gaucher’s disease
Increased
68
Specific enzyme deficiency in Gaucher's disease
glucocerosidase deficiency
69
Level of ACP in Thrombocytopenia and ITP
Increased (due to platelet destruction)
70
Bilirubin derived from non-defective and immature RBCs or hepatic cytochromes
Shunt Bili
71
Lactate Dehydrogenase (LD) method 1
Berger Brada
72
Forward or direct LD method involving pH 8.8 at 340 nm
Wacker Method
73
The Wacker method measures the amount of
hydrogen ion formed
74
Backward, indirect, or reverse LD method involving pH 7.2 at 340 nm
Wroblewski LaDue
75
The Wroblewski LaDue method measures the amount of
NAD formed
76
Compare the speed of Wacker and Wroblewski LaDue
Wroblewski LaDue is 2x more rapid
77
Reaction formula for Wacker method
Lactate + NAD+ → Pyruvate + NADH + H+
78
Reaction formula for Wroblewski LaDue method
Pyruvate + NADH + H+ → Lactate + NAD+
79
Direct CK method involving pH 9.0 at 340 nm
Tanzer-Gilvarg
80
Backward, indirect, or reverse CK method involving pH 6.8
Oliver Rosalki
81
The most common and more rapid (2X) method for CK
Oliver Rosalki
82
Biochemical marker formula used to identify the cause of liver damage
De Ritis Ratio (AST / ALT)
83
Half-life of AST in the blood
18 hours
84
Half-life of ALT in the blood
36 hours
85
A De Ritis ratio of > 2.0, especially > 3.0, is highly suggestive of
alcoholic liver disease
86
A De Ritis ratio of < 1.0 is typically seen in
acute viral hepatitis and non-alcoholic fatty liver disease (NAFLD)
87
In non-alcoholic liver disease, a De Ritis ratio of > 1.0 may indicate a more advanced stage such as
cirrhosis
88
Clinical significance of Acid phosphatase (ACP)
Prostatic carcinoma
89
Clinical significance of Alanine aminotransferase (ALT)
Hepatic disorder
90
Clinical significance of Aldolase (ALD)
Skeletal muscle disorder
91
Clinical significance of Alkaline phosphatase (ALP)
Hepatic disorder and Bone disorder
92
Clinical significance of Amylase (AMY)
Acute pancreatitis
93
Clinical significance of Angiotensin-converting enzyme (ACE)
Blood pressure regulation
94
Clinical significance of Aspartate aminotransferase (AST)
Myocardial infarction, Hepatic disorder, and Skeletal muscle disorder
95
Clinical significance of Chymotrypsin (CHY)
Chronic pancreatitis insufficiency
96
Clinical significance of Creatine kinase (CK)
Myocardial infarction and Skeletal muscle disorder
97
Clinical significance of Elastase-1 (E1)
Chronic pancreatitis insufficiency
98
Clinical significance of Glucose-6-phosphate dehydrogenase (G-6-PD)
Drug-induced hemolytic anemia
99
Clinical significance of Glutamate dehydrogenase (GLD)
Hepatic disorder
100
Clinical significance of γ-Glutamyltransferase (GGT)
Hepatic disorder
101
Clinical significance of Glutathione-S-transferase (GST)
Hepatic disorder
102
Clinical significance of Glycogen phosphorylase (GP)
Acute myocardial infarction
103
Clinical significance of Lactate dehydrogenase (LD)
Myocardial infarction, Hepatic disorder, and Hemolysis Carcinoma
104
Clinical significance of Lipase (LPS)
Acute pancreatitis
105
Clinical significance of 5'-Nucleotidase
Hepatic disorder
106
Clinical significance of Pyruvate kinase (PK)
Hemolytic anemia
107
Clinical significance of Trypsin (TRY)
Acute pancreatitis
108
this is the most accepted theory for enzymes
induced fit theory
109
amylase measurements include
Saccharogenic- formation of a reduced sugar
Amyloclastic- breakdown of starch
Coupled enzymatic
Ccolorimetric
110
most common and ference method for lipase
Cheryy and Crandall
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