1. an enzyme that catalyzes the 1.

Ligase or synthetase
bonding together of t molecules
into one with the participation
ATP.
2. an enzyme that catalyzed 2. Isomerase
isomerization
3. is an enzyme that catalyzes a 3. Hydrolase
hydrolysis reaction in which the
addition of a water molecule to a
bond causes the bond to break
4. is an enzyme that catalyzes an 4. Oxidoreductase
oxidation-reduction reaction.
5. is an enzyme that catalyzes the 5. Lyase
addition of a group to a double
bond or the removal of a group to
form a double bond in a manner
that does not involve hydrolysis
or oxidation.
6. breaking of glycosidic bonds in 6. Proteases
oligo-and polysaccharides
7. breaking of ester linkages in 7. lipases
triacylglycerols
8. effects the removal of the 8. dehydrogenase
components of water from the
double bond
9. decreases the number of C-O 9. Organic reduction
bonds and/or increases the
number of C-H bond
10. effects the addition of the 10. Hydratase
components of water to a double
bond
11. conversion of D isomer to L 11. Racemases
isomer, or vice versa
12. introduction of double bond 12. Dehydrogenase
(oxidation) by formal removal of
to H atoms from substrate, the H
being accepted by coenzyme
13. hydrolysis of sugar-phosphate 13. nucleases
ester bonds in nucleic acid
14. Subclasses of lyases 14. - dehydratases
- decarboxylases
- deaminases
- hydratases
15. Subclasses of ligases 15. - synthetases
- Carboxylases
16. oxidation of a substrate 16. oxidases
17. reduction of a substrate 17. reductases
18. transfer of a functional group 18. Mutases
from one position to another in
the same molecule
19. formation of new bond between 19. Synthetases
two substrates, with participation
of ATP
20. hydrolysis of phosphate-ester 20. Phosphatases
bond
21. transfer of an amino group 21. Transaminases
between substrates
22. removal of NH3 from a substrate 22. deaminases
23. Subclasses of hydrolases 23. - lipases
- proteases
- nucleases
- carbohydrases
- phosphatases
24. formation of new bond between a 24. Carboxylases
substrate and CO2, with
participation of ATP
25. removal of H20 from a substrate 25. dehydratases
26. addition of H20 to a substrate 26. hydratases
27. hydrolysis of amide linkages in 27. proteases
proteins
28. subclasses of transferases 28. - transaminases
- kinases
29. removal of CO2 from a substrate 29. Decarboxylases
30. subclasses of isomerases 30 - racemases
- mutases
31. subclasses of oxidoreductase 31. - oxidases
- reductases
- dehydrogenase
32. transfer of a phosphate group 32. kinases
between substrate
33. enzyme molecules contain a 33. active site
special pocket or cleft called
34. are protein catalysts that increase 34. enzymes
the velocity of a chemical
reaction.
35. is the reactant in an 35. Substrate
enzyme-catalyzed reaction
36. Main classes of enzymes 36. - oxidoreductase
- transferases
- hydrolases
- lyases
- isomerases
- ligases
37. is the region of an enzyme where 37. active site
substrate molecules bind and
undergo a chemical reaction.
38. residues that catalyze a reaction 38. catalytic site
of that substrate
39. The active site consists of 39. binding site
residues that form temporary
bonds with the substrate.
40. allows for small changes in the 40. Induced fit model
shape or geometry of the active
site of an enzyme to accomodate
a substrate.
41. the number of molecules of 41. turnover number / kcat
substrate converted to product
per enzyme molecule per second
is called
42. The active site in the enzyme has 42. Lock and key model
fixed, rigid geometrical
conformation.
43. is the intermediate reaction 43. Enzyme-substrate complex
species that is formed when a
substrate binds to the active site
of an enzyme.
44. 4 types of specificity 44. - absolute
- group
- linkage
- stereochemical
45. is an enzyme that has a non 45. conjugated enzyme
protein part in addition to a
protein part.
46. refers to the active enzyme with 46. holoenzyme
its non protein component.
47. 2 types of ESC or models of 47. - Lock and key model
enzyme activity - induced fit model
48. 2 types of active site 48. - binding site
- catalytic site
49. is an enzyme composed only of 49. simple enzyme
protein (amino acid chains)
50. the enzyme without its non 50. apoenzyme
protein moiety or the protein part
of the conjugated enzyme
51. Coenzymes that only transiently 51. cosubstrate
associate with the enzyme
52. If the non protein moiety is a 52. cofactor
metal ion, it is a
53. If it is a small organic molecule 53. coenzyme
54. If the coenzyme is permanently 54. Prosthetic group
associated with the enzyme and
returned to its original form
55. enzyme will catalyze only one 55. Absolute
reaction
56. the enzyme will act on a 56. stereochemical
particular stereoisomer.
57. Only substrates with a 57. lock and key model
complementary geometry can be
accommodated at such site
58. contains amino acid side chains 58. active site
that participate in substrate
binding and catalysis
59. a conformational change in the 59. induced fit
enzyme
60. systematic name of lactate 60. NAD+ oxidoreductase
61. the enzyme will act only on 61. group specificity
molecules that have a specific
functional group
62. The enzyme will act on a 62. Linkage
particular type of chemical bond,
irrespective of the rest of the
molecular structure.
63. Example of group specificity 63. Carboxypeptidase
enzyme
64. Example of linkage specificity 64. Phosphatases
enzyme
65. Absolute 65. Catalase enzyme
66. Stereochemical 66. L - amino acid oxidase
67. 2 general structural classes: 67. - simple enzymes
- conjugated enzymes
68. is the difference in free energy 68. Free energy of activation
between the reactant and T,
where the high-energy
intermediate is formed during the
conversion of reactant to product.
69. factors responsible for the 69. - transition-state stabilization
catalytic efficiency of enzymes: - catalysis
- visualization of the transition
state
70. Virtually all chemical reactions 70. free energy of activation
have an energy barrier
separating the reactant and the
products. This barrier is called
the
71. is a complex molecular machine 71. active site
employing a diversity of chemical
mechanisms to facilitate the
conversion of substrate to
product.
72. Factors affecting enzymatic 72. - Substrate concentration
activity: - Temperature
- pH
- Enzyme concentration
73. is the number of substrate 73. rate or velocity of a reaction
molecules converted to product
per unit time
74. means that all enzyme active site 74. Saturation
were fully occupied and so the
reaction rate remains constant
75. is the temperature at which an 75. Optimum temperature
enzyme exhibits maximum
activity.
1. enzyme that aids in the digestion 1. lipase
of fat.
2. an enzyme found in the liver, 2. g-glutamyl transpeptidase
kidney, and pancreas
3. is found in both cardiac and 3. Troponin T
skeletal muscle
4. found in the liver 4. Aspartate Aminotransferase/
serum glutamic oxaloacetic
transaminases
5. are most often used in the 5. Serum Amylase levels
diagnosis of acute pancreatitis.
6. It is also located in the 6. Alanine Aminotransferase
myocardial, muscle, and renal
tissue.
7. useful in the diagnosis of 7. Lipase
pancreatitis and is considered a
more specific marker for acute
pancreatitis than amylase.
8. are sensitive markers of cardiac 8. Troponin I and T
injury
9. are present in liver tissue, and 9. LDH4 and LDH5
elevations may be seen in liver
disease such as hepatitis and
cirrhosis.
10. is an enzyme that is found 10. Creatine Kinase
primarily in skeletal and cardiac
muscle and in smaller fractors in
the brain
11. important maker in the diagnosis 11. Cardiac tissue (CK-MB)
of acute myocardial infarction
(AMI)
12. is solely found in the cardiac 12. Troponin I
muscle
13. may be useful in the diagnosis of 13. LDH1 and LDH2
myocardial infarction
14. for the diagnosis of liver disease 14. Aspartate Aminotransferases
15. Troponin levels begin to rise 15. 4 hours of onset of chest pain
within
16. May be seen in alcoholic liver 16. g-glutamyl transpeptidase
disease, metastatic liver disease..
17. considered a specific marker for 17. Alanine Aminotransferase
liver disease
18. are useful in the diagnosis and 18. g-glutamyl transpeptidase
monitoring of alcohol liver
disease
19. Levels of troponin should be 19. admission within 8 to 12 hours
drawn on ________ within ____.
20. The majority of amylase is 20. pancreas and salivary glands
produced in the _________
21. lesser amounts are secreted by 21. fallopian tubes, lungs, thyroid, and
the ________. tonsils
22. Biochemically important 22. - Creatine kinase
enzymes: - cardiac troponin
- gastrointestinal test
23. enzyme involved in the 23. lactate dehydrogenase
interconversion of lactate and
pyruvate
24. proposed a simple model that 24. Leonor Michaelis and Maude
accounts for most of the features Menten
of enzyme-catalyzed reactions.
25. the Michaelis constant 25. Km
26. describes how reaction velocity 26. Michaelis-Menten equation
varies with substrate
concentration.
27. an enzyme tof protein digestion in 27. Chymotrypsin
the intestine, includes general
base, general acid, and covalent
catalysis