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BCHMLS1 > ENZYMOLOGY > Flashcards

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
Q
  • These are the several distinct forms of enzymes
  • Important in the diagnosis of specificity
A

ENZYME VARIANT

26
Q

Enzymes of similar activity typically appearing in specific tissue, organs and cell organelles of organisms and the same species

A

ISOENZYMES

27
Q

Same enzymatic activity, which are specie specific for different biological species

A

HETEROENZYMES

28
Q

Genetically transmitted enzymes

A

ALLOENZYMES

29
Q

Generally secreted by liver into the plasma

A

Plasma Specific Enzymes

30
Q

Enzymes that do not have specific function in plasma

A

Non-plasma specific enzymes

31
Q

Enzymes secreted in plasma at a very high rate but are rapidly

A

Enzyme of secretion

32
Q

Enzymes that carry out their functions within the cells

A

Enzymes associated with cellular metabolism

33
Q

These are enzymes found only in the cell sap
Found only in one location

A

Unilocular enzymes

34
Q

These are enzymes that are found in the mitochondria and cell sap

A

Bilocular Enzyme

35
Q

this refers to the activation energy

A

Energy

36
Q

E + S = commonness and sameness between

A

Molecular compatibility

37
Q

refers to the number of enzymes or substrates that can be reacted

A

pace availability

38
Q

refers to the particular enzyme catalyzing a specific substrate

A

Specificity

39
Q

refers to the active site being complementary in shape and size of the substrate

A

Lock and Key

40
Q

refers to the enzyme changing in shape during binding with substrate. After binding, the shape of the enzyme complements with the binding site

A

Induced Fit model

41
Q

Enzyme concentration is fixed and the substrate concentration is varied

A

First Order Kinetics

42
Q

The rate depends on the enzyme concentration and independent of substrate concentration

A

Zero Order Kinetics

43
Q

An increase in the enzyme concentration result to an increase in the catalytic activity of the enzyme

A

Enzyme Concentration

44
Q

the point at which the enzyme molecule is capable of catalyzing the substrate

A

Optimum temperature

45
Q

Optimum temperature

A

30-37C or 37-40C

46
Q

refers to the increased reaction rate for every 10C increase (rate of reaction is doubled)

A

Q10 value

47
Q

the point at which the reaction rate is greatest

A

Optimum pH

48
Q

many enzymes show maximum activity

A

pH 7-8

49
Q

ii. pepsin is active at __ and ALP at __

A

1.5 and 10.5

50
Q

from ionic bridges to help bind in the substrate to the active site

A

Activators

51
Q

Substances that decrease the rate of enzyme reaction if these are present in the reaction system

A

Inhibitors

52
Q

Binds to the active site, blocking the access of the substrate to the enzyme

A

Competitive Inhibition

53
Q

Binds elsewhere on the enzyme causing change in shape that interferes with substrate binding

A

Non-competitive)

54
Q

inhibitors bind with the ES completely; no product formed

A

Uncompetitive

55
Q

When inhibitors are possible removed from the system and enzyme is fully restored
- can be separated

A

Reversible inhibition

56
Q

When inhibitors combine covalently with the enzyme

A

Irreversible inhibition

57
Q

Causes competition between substrate molecules for a single binding site

A

Excess substrate

58
Q

A product of reaction may itself be an inhibitor of the forward reaction

A

Product of Reaction

59
Q

These must be present at the proper concentration for many enzyme reactions to take place

A

Coenzyme concentration

60
Q

These are essentially coenzymes that firmly bind with enzymes

A

Prosthetic Group

BCHMLS1 (1 decks)

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