ENZYMOLOGY Flashcards

1
Q

catalysts bind reactants (substrates), convert them to products and release the products.

A

ENZYMES

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2
Q

serve as recyclable shuttles that transport many substrates form one point within the cell to another

A

COENZYME

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3
Q

it is where the transformation of the substrate takes place

A

ACTIVATORS

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4
Q

a biochemically active compound formed by the combination of an enzyme with a coenzyme

A

HALOENZYME

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5
Q

is a protein part that binds to a non-protein cofactor to form an active conjugated enzyme known as the haloenzyme

A

APOENZYME

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6
Q

are tightly and stably incorporated into protein’s structure by covalent or noncovalent bond

A

PROSTHETIC GROUP

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7
Q

use a metal cation as factor in the enzyme active site

A

METALOENZYME

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8
Q

enzyme catalyst that bind reactants

A

SUBSTRATE

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9
Q

convert them to products and release the products

A

PRODUCT

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10
Q

It refers to the molecular/structural arrangement of enzyme molecule

A

ENZYME STRUCTURE

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11
Q

It is where the transformation of the substrate takes place

A

ACTIVE STE

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12
Q

refers to the sequence of amino acids joined by peptide bonds

A

PRIMARY STRUCTURE

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13
Q

conformation of the steric arrangement or conformation of the segments of polypeptide chain

A

SECONDARY STRUCTURE

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14
Q

arises from the interactions among side chains/groups of the polymer chain; folded structure of an enzyme

A

TERTIART STRUCTURE

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15
Q

refers to the relationship between subunits

A

QUATERNARY STRUCTURE

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16
Q

The International Union of Biochemistry (IUB) enzyme commission categorized all enzymes into 6 classes

A

Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases

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17
Q

Enzymes catalyzing oxidation and reduction reactions

A

OXIDOREDUCTASES

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18
Q

addition of hydrogen to a double bond

A

REDUCTION

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19
Q

removal of hydrogen to cleave a double bond

A

OXIDATION

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20
Q

Enzymes that move and interact group of atoms from one molecule to another (amine or PO4 group)

A

TRANSFERASES

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21
Q

Enzymes involved in the splitting of molecules with water as a part of the reaction process

A

HYDROLASES

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22
Q

Enzymes responsible for splitting molecules (lysis)

A

LYASES

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23
Q

Enzymes responsible for the conversion of one isomer to another

A

ISOMERASES

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24
Q

Enzyme causing bond formation between two molecules to form a longer molecule

A

LIGASES

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25
- These are the several distinct forms of enzymes - Important in the diagnosis of specificity
ENZYME VARIANT
26
Enzymes of similar activity typically appearing in specific tissue, organs and cell organelles of organisms and the same species
ISOENZYMES
27
Same enzymatic activity, which are specie specific for different biological species
HETEROENZYMES
28
Genetically transmitted enzymes
ALLOENZYMES
29
Generally secreted by liver into the plasma
Plasma Specific Enzymes
30
Enzymes that do not have specific function in plasma
Non-plasma specific enzymes
31
Enzymes secreted in plasma at a very high rate but are rapidly
Enzyme of secretion
32
Enzymes that carry out their functions within the cells
Enzymes associated with cellular metabolism
33
These are enzymes found only in the cell sap Found only in one location
Unilocular enzymes
34
These are enzymes that are found in the mitochondria and cell sap
Bilocular Enzyme
35
this refers to the activation energy
Energy
36
E + S = commonness and sameness between
Molecular compatibility
37
refers to the number of enzymes or substrates that can be reacted
pace availability
38
refers to the particular enzyme catalyzing a specific substrate
Specificity
39
refers to the active site being complementary in shape and size of the substrate
Lock and Key
40
refers to the enzyme changing in shape during binding with substrate. After binding, the shape of the enzyme complements with the binding site
Induced Fit model
41
Enzyme concentration is fixed and the substrate concentration is varied
First Order Kinetics
42
The rate depends on the enzyme concentration and independent of substrate concentration
Zero Order Kinetics
43
An increase in the enzyme concentration result to an increase in the catalytic activity of the enzyme
Enzyme Concentration
44
the point at which the enzyme molecule is capable of catalyzing the substrate
Optimum temperature
45
Optimum temperature
30-37C or 37-40C
46
refers to the increased reaction rate for every 10C increase (rate of reaction is doubled)
Q10 value
47
the point at which the reaction rate is greatest
Optimum pH
48
many enzymes show maximum activity
pH 7-8
49
ii. pepsin is active at __ and ALP at __
1.5 and 10.5
50
from ionic bridges to help bind in the substrate to the active site
Activators
51
Substances that decrease the rate of enzyme reaction if these are present in the reaction system
Inhibitors
52
Binds to the active site, blocking the access of the substrate to the enzyme
Competitive Inhibition
53
Binds elsewhere on the enzyme causing change in shape that interferes with substrate binding
Non-competitive)
54
inhibitors bind with the ES completely; no product formed
Uncompetitive
55
When inhibitors are possible removed from the system and enzyme is fully restored - can be separated
Reversible inhibition
56
When inhibitors combine covalently with the enzyme
Irreversible inhibition
57
Causes competition between substrate molecules for a single binding site
Excess substrate
58
A product of reaction may itself be an inhibitor of the forward reaction
Product of Reaction
59
These must be present at the proper concentration for many enzyme reactions to take place
Coenzyme concentration
60
These are essentially coenzymes that firmly bind with enzymes
Prosthetic Group