Enzymology Flashcards
1
Q
Enzymes measures from?
A
12 kilo Daltons to 1,000 kilo Daltons
2
Q
They are responsible for the different reactions in living matter necessary during digestion, metabolism, respiration, energy release and energy transfer in all metabolic reactions.
A
Enzymes
3
Q
A specific region in enzyme which interacts with its substrate.
A
Active site
4
Q
The substance acted upon by an enzyme.
A
Substrate
5
Q
It is derived from a transformed substrate
A
Product
6
Q
a cavity (other than the active site) that may bind regulator molecules
and thereby be significant to the basic enzyme structure
A
Allosteric site
7
Q
Are invariably complex proteins
A
Enzymes
8
Q
Enzymes are generally soluble in?
A
Water, glycerol and dilute alcohol
9
Q
Enzymes are ____ in nature and are not _____
A
Colloidal; dialyzable
10
Q
Enzymes function with a?
A
Cofactor
11
Q
True or false: Enzymes are consumed and produced during the course of a reaction
A
Very very False
12
Q
True or false: Enzymes do not cause reactions to take place but they expedite reactions.
A
Very very true
13
Q
Are complex proteins
A
Enzymes
14
Q
Means that they do not affect the acid-base balance of the body
A
Amphoteric
15
Q
They are highly specific for the reaction they catalyze and only produce the expected produces from given reactants or substrates.
A
Enzymes
16
Q
True or false: Enzymes are easily denatured
A
Very very true
17
Q
Enzymes are synthesized in ___ state.
A
Inactive
18
Q
It is a high energy state
A
Transition state
19
Q
Is the Energy required to achieve or go to the transition state
A
Activation energy
20
Q
What decreases the energy required to get a reaction started?
A
Enzyme
21
Q
True or false: Enzymes lower energy barrier by forcing reacting molecules through different transition state.
A
true na true for you
22
Q
True or false: the higher the free energy change for the transition barrier the slower the reaction rate is.
A
Very true ka diyan
23
Q
Are non-protein molecule, necessary for enzyme activity
A
Cofactor
24
Q
Are inorganic cofactors
A
Activators
25
Are organic cofactors
Coenzyme
26
Is a coenzyme bound tightly to the enzyme
Prosthetic group
27
It is secreted from the organ of production in an
inactive form (digestive enzymes)
Proenzyme/Zymogen
28
Is the enzyme portion without cofactor
Apoenzyme
29
Combination of Apoenzyme + coenzyme
Holoenzyme
30
Holoenzyme is the combination of?
Apoenzyme + coenzyme
31
Are inorganic activators existing as part of the enzyme
molecule usually consist of earth metals
Metalloenzyme
32
Examples of earth metals found in metalloenzymes
Iron, calcium, magnesium
33
Enzyme structure that is the specific amino acid sequence
Primary structure
34
Are the most important configurations in enzyme structure because it is responsible for characteristics like coiling and folding which results to formation of active site
Secondary and Tertiary structure
35
It is the twisting of the polypeptide chains
Secondary structure
36
The folding of the chains (interactions among the side
chains/groups of chains)
Tertiary structure
37
The spatial relationship between
the subunits
Quaternary structure
38
Where final adjustments happens to molecules before it becomes active
Quaternary structure
39
Are different molecular forms of enzymes that may be isolated from the same or different tissues but are of similar activity.
Isoemzymes
40
LD2 - H3M is found in?
(clue: H, R, R)
heart, RBC & renal tissues
41
LD3 - H2M2 is found in?
(Clue: L, L, S, P)
Lungs, lymphocytes, spleen, pancreas
42
LD1 - H4 is found in?
(Clue: H, R, R)
heart, RBC & renal tissues
43
LD4 - HM3 is found in?
(Clue: L, S)
liver, skeletal muscles
44
LD5 - M4 is found in?
(Clue: L, S)
liver, skeletal muscles
45
CK-MB found in?
(Clue: H, S)
Heart and skeletal muscle
46
CK-MM found in?
(Clue: H, S)
Heart and Skeletal muscle
47
CK-BB found in?
(Clue: B, B, L, P)
Brain, Bladder, Lung, Prostate...
48
same enzymatic activity which are specie specific for different biological species
Heteroenzyme
49
Are Genetically transmitted enzymes important in defining the biochemical characteristics of an individual
Alloenzyme
50
Present only in some selected individuals of the same species
Alloenzyme
51
Has practical value in forensic medicine and genetics
Alloenzyme
52
Origin of enzymes that is secreted in the liver and released in the plasma. Exert function in plasma
Plasma Specific Enzymes
53
Origin of enzymes that has no specific function in plasma
Non-Plasma Enzymes
54
The two classes of Non-Plasma Enzymes
Enzymes of secretion
Enzymes associated with cellular metabolism
55
Based on distribution:
Can be seen in Cell sap or one location only
Unilocular
56
Based on distribution:
Can be seen in mitochondria and cell sap
Bilocular
57
Nomenclature based on organ/ observation/experiences
Empirical names
58
First digit:______
class of the enzyme (1 - 6)
59
Nomenclature: With 4 digits separated by decimal points
EC numerical code
60
Nomenclature suitable for everyday use
Trivial or Practical Name
61
Fourth digit:______
serial number that is specific to each enzyme in a sub-subclass
62
Second and Third digits: _______
subclass and sub- subclass
63
Simplification of naming by using acronyms and Uppercase abbreviation of enzymes
Trivial or Practical Name
64
Nomenclature Associated unique numerical code designation
Systematic name
65
Nomenclature: define the substrate acted upon and describe the nature of the reaction catalyzed
Systematic name
66
Catalyze oxidation and reduction reactionsbetween 2 substrates
OXIDOREDUCTASES
67
Catalyze the joining of 2 substrate molecules usually with energy supplied by the cleavage of an ATP
LIGASES
68
Catalyze the interconversion of one isomer to another by molecular rearrangements
ISOMERASES
69
Catalyze hydrolysis of variety of bonds
HYDROLASES
70
Catalyze removal of groups from substrates without hydrolysis
LYASES
71
Catalyze the transfer of an intact group of atoms (amine or phosphate group) from one substrate to another
TRANSFERASES
72
Most of these enzymes are important in assessing heart attacks and liver problems
OXIDOREDUCTASES
73
Most are assayed in skeletal muscle disorders
LYASES
74
Most of these enzymes are important in assessing liver damage and myocardial infarction
TRANSFERASES
75
the particular enzyme catalyzing a specific substrate
Specificity
76
the active site of the enzyme is complementary in conformation to the substrate, so that the enzyme and the substrate recognize one another
Lock and Key Theory
77
number of enzymes or substrates that can be reacted
Space availability
78
commonness /sameness of enzyme and substrate
Molecular compatibility
79
The enzyme changes shape upon binding the substrate, so that the conformation of substrate and enzyme protein are only complementary upon the binding reaction.
Induced fit theory
80
activation energy
Energy
81
Enzyme concentration is fixed and the substrate concentration is varied
FIRST ORDER KINETICS
82
At low substrate, the rate is directly
proportional to substrate concentration
SUBSTRATE CONCENTRATION
83
Reaction rate is dependent on substrate concentration
FIRST ORDER KINETICS
84
With excess substrate, the rate is a direct measure to the amount of enzyme present
SUBSTRATE CONCENTRATION
85
Im Substrate concentration At high substrate, the rate is _____
constant
86
condition where the enzymatic reaction is allowed to take place
TIME
87
Reaction rate is dependent on enzyme concentration
ZERO ORDER KINETICS
88
Direct Relationship
ENZYME CONCENTRATION
89
When maximum velocity is reached, the rate of increase in velocity is “0”
ZERO ORDER KINETICS
90
Increase of 10 degree C doubles the rate of enzyme activity
TEMPERATURE
91
Form ionic bridges to help bind the substrate to the active site
Activators
92
bind to the ES complex
Uncompetitive Inhibitors
93
bind to the active site of the enzyme
Competitive Inhibitors
94
bind at place other than the active site = change in shape
Non-Competitive Inhibitors
95
Can be separated via physical dialysis, gel filtration
Reversible Inhibition
96
Inhibitors combine covalently with the enzyme
Irreversible Inhibition
97
may itself be an inhibitor of the forward reaction
Product of Reaction
98
causes competition between substrate molecules for a single binding site
Excess substrate
99
These are essentially coenzymes that firmly bind with enzymes
Prosthetic Group
100
These must be present at the proper concentration for many enzyme reactions to take place
COENZYME Concentration
101
enzyme combines with only 1 substrate and catalyzes only the one corresponding reaction
ABSOLUTE SPECIFICITY
102
It refers to the disruption of the structure of enzyme molecule (3-dimensional structure) that leads to the loss of enzyme activity
ENZYME DENATURATION
103
Denaturation may be reversed if the reaction process ______ too far and if ________
has not gone; the denaturing agent is removed
104
when an enzyme acts only on the specific isomer of a certain compound
STEREOISOMERIC
105
when some enzymes act on all substrates containing a particular chemical group
GROUP SPECIFICITY
106
Multiple measurements (absorbance change), At specific time interval , Continuous-recording, spectrophotometer
CONTINUOUS-MONITORING
107
Enzymes cause antibody production when injected to animals to which they are foreign
IMMUNOASSAYS
108
The reactants are combined, the reaction proceeds for a designated time, Measure amount of reaction
FIXED-TIME
109
least preferred specimen, inhibitorytoenzymeactivity
USE OF PLASMA
110
presence of intracellular enzyme causes an increase in enzyme concentration
HEMOLYSIS
111
In timing, prolonged time of reaction increases ________
product formation
112
Prolonged time of incubation leads to _____ and _______
denaturation; inhibition of enzyme reaction
