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1
A compound, usually a protein, that acts as a catalyst for a biochemical reaction
Enzymes
2
Most enzymes are globular proteins
Enzymes
3
Enzymes undergo all the reactions of proteins including ________
denaturation
4
Ability to speed up reaction
Enzymes
5
factors that affect enzyme activity
Temperature (too hot = denature | too cold = denature)
Alterations in pH
denaturation
6
composed only of protein (amino acid chains) (protein part)
simple enzyme
7
it has a nonprotein part in addition to a protein part (nonprotein & protein part) , what is the non protein part and protein part?
conjugated Enzyme , Apoenzyme – protein part, cofactor- non protein part
8
Apoenzyme + Cofactor =
Holoenzyme
9
small organic molecule that serves as a cofactor in a conjugated enzyme
Coenzyme
10
what are the Typical inorganic ion cofactors: (Activators)
- Zn
- Mg
- Mn
- Fe
- Cu
- K
- Na
11
Oxidoreductase

Is an energy that catalyzes an oxidation-reduction reaction .
Requires a cofactor that is oxidized or reduced as the substrate is reduced or oxidized

only 1st statement is correct
only 2nd statement is correct
both statements aare correct
both statements are incorrect
both are wrong

Is an enzyme that catalyzes an oxidation-reduction reaction .
Requires a coenzyme that is oxidized or reduced as the substrate is reduced or oxidized
12
what type of Major Classes of Enzymes that Lactate Dehydrogenase belong?
Oxidoreductase
13
An enzyme that catalyzes the transfer of a functional group from one molecule to another
Transferase
14
catalyzes the transfer of an amino group from one molecule to another
transaminase
15
play a major role in metabolic energy-production reactions, catalyze the transfer of a phosphate group from adenosine
triphosphate (ATP) to give adenosine diphosphate (ADP) and a phosphorylated product.
Kinases
16
An enzyme that catalyzes a hydrolysis reaction in which the addition of a water molecule to a bond causes the
bond to break
Hydrolase
17
effect the breaking of glycosidic bonds in oligo- and polysaccharides
Carbohydrases
18
effect the breaking of peptide linkages in proteins
proteases
19
effect the breaking of ester linkages in triacyglycerols.
lipases
20
An enzyme that catalyzes the 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
Lyase
21
effects the removal of the components of water from a double bond
dehydratase
22
effects the addition of the compositions of water to a double bond.
hydratase
23
An enzyme that catalyzes the isomerization (rearrangement of atoms) of a substrate in a reaction, converting it
into a molecule isomeric with itself
Isomerase
24
An enzyme that catalyzes the bonding together of two molecules into one with the participation of ATP
Ligase
25
what type of Six Major Classes of Enzymes is Nucleoside monophosphate kinase (NMP kinase) belongs?


Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases , Ligases
transferases
26
what type of Six Major Classes of Enzymes is Chymotrypsin belongs?


Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases , Ligases
hydrolases
27
what type of Six Major Classes of Enzymes is Fumarase belongs?


Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases , Ligases
lyases
28
what type of Six Major Classes of Enzymes is Triose phosphate isomerase belongs?


Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases , Ligases
isomerases
29
what type of Six Major Classes of Enzymes is Aminoacyl-tRNA synthetase belongs?


Oxidoreductases, Transferases, Hydrolases, Lyases, Isomerases , Ligases
ligases
30
relatively small part of an enzyme’s structure that is actually involved in catalysis.
Active Site
31
intermediate reaction species that is formed when a substrate binds
Enzyme Substrate Complex (ES)
32
The active site in the enzyme has a fixed, rigid geometrical conformation. Only substrates with a complementary
geometry can be accommodated at such a site, much as a lock accepts only certain keys
Lock - and - Key Model
33
Extent to which an enzyme’s activity is restricted to a specific substrate, a specific group of substrate, a specific
type of chemical bond or a specific type of reaction.
Enzyme Specificity
34
Allows for small changes in the shape or geometry of the active site of an enzyme to accommodate a substrate. A
good analogy is the changes that occur in the shape of a glove when a hand is inserted into it.
Induced - Fit Model
35
Enzyme will catalyze only one reaction. This most restrictive of all specificities is not common
Absolute Specificity
36
is an enzyme with absolute specificity
catalase
37
Enzyme will act on a particular type of chemical bond, irrespective of the rest of the molecular structure
Linkage Specificity
38
is the most
general of the common specificities.
Linkage specificity
39
Enzyme will act on a particular stereoisomer
Stereochemical Specificity
40
slows or stops the normal catalytic function of an enzyme by binding to it.
Enzyme Inhibitor
41
A molecule that sufficiently resembles an enzyme substrate in shape and charge distribution that it can compete
with the substrate for occupancy of the enzyme’s active site.
Competitive Inhibitor
42
A molecule that decreases enzyme activity by binding to a site on an enzyme other than the active site
Non-Competitive Inhibitor
43
A molecule that inactivates enzymes by forming a strong covalent bond to an amino acid side- chain group at the
enzyme’s active site
Irreversible Inhibitor
44
what is Selected Blood Enzyme Assays use in Diagnostic Medicine "heart disease, liver disease "




lactate Dehydrogenase (LDH), Creatinine Phosphokinase (CPK)), Aspartate Transaminase (AST), Alanine Transaminase (ALT), Gamma-glutamyl Transpeptidase (GGTP), Alkaline Phosphatase (ALP)
LDH
45
what is Selected Blood Enzyme Assays use in Diagnostic Medicine
"heart disease"





lactate Dehydrogenase (LDH), Creatinine Phosphokinase (CPK)), Aspartate Transaminase (AST), Alanine Transaminase (ALT), Gamma-glutamyl Transpeptidase (GGTP), Alkaline Phosphatase (ALP)
CPK
46
what is Selected Blood Enzyme Assays use in Diagnostic Medicine
"bone ,liver disease"



lactate Dehydrogenase (LDH), Creatinine Phosphokinase (CPK)), Aspartate Transaminase (AST), Alanine Transaminase (ALT), Gamma-glutamyl Transpeptidase (GGTP), Alkaline Phosphatase (ALP)
ALP
47
what is Selected Blood Enzyme Assays use in Diagnostic Medicine
"heart disease, liver disease, muscle damage "


lactate Dehydrogenase (LDH), Creatinine Phosphokinase (CPK)), Aspartate Transaminase (AST), Alanine Transaminase (ALT), Gamma-glutamyl Transpeptidase (GGTP), Alkaline Phosphatase (ALP)
AST or ALT
48
what is Selected Blood Enzyme Assays use in Diagnostic Medicine
"heart disease, liver disease"

lactate Dehydrogenase (LDH), Creatinine Phosphokinase (CPK)), Aspartate Transaminase (AST), Alanine Transaminase (ALT), Gamma-glutamyl Transpeptidase (GGTP), Alkaline Phosphatase (ALP)
GGTP
49
k1 or k2

is found in dark green, leafy vegetables
k1
50
k1 or k2


synthesized by bacteria that grow in colon
k2
51
what type of vitamin

protect vit A from undergoing oxidation
vitam e
52
what type of vitamin

- Vision
- Regulating Cell Differentiation
- Maintenance of the Health of Epithelial Tissue
vitamin a
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