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ENZYMES (MOD 4) > CLASS AND PROPERTIES OF ENZYMES > Flashcards

CLASS AND PROPERTIES OF ENZYMES Flashcards

1
Q

carbohydrase, proteases and lipases are examples of?

A

HYDROLASE

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2
Q

CLASSIFICATION OF ENZYMES

A

OXIDOREDUCTASE
TRANSFERASE
HYDROLASE
LYASE
ISOMERASE
LIGASE / SYNTHETASE

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3
Q

breaking of glycosidic bonds in oligo- and polysaccs

A

CARBOHYDRASE

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4
Q

enzyme that catalyzes an oxidation-reduction reaction

A

OXIDOREDUCTASE

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5
Q

Lactate dehydrogenase is an example of?

A

OXIDOREDUCTASE

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5
Q

breaking of peptide linkages in protein

A

PROTEASES

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6
Q

breaking of ester linkages in TAG

A

LIPASES

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7
Q

Catalyzed reaction:
lactic acid + NAD = pyruvic acid + NADH + H+

A

LACTATE DEHYDROGENASE

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8
Q

enzyme that catalyzes the addition of a grp to a double bond

A

LYASE

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9
Q

increases the number of C-O bonds and/or decreases no. of C-H bonds

A

ORGANIC OXIDATION

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10
Q

removal of a group to form a double bond in a manner that does not involve hydrolysis or oxidation

A

LYASE

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11
Q

decreases the number of C-O bonds and/or increases no. of C-H bonds

A

ORGANIC REDUCTION

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11
Q

dehydratase and hydratase are examples of?

A

LYASE

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12
Q

enzyme that catalyzes the transfer of functional grp other than hydrogen frm one mol. to another

A

TRANSFERASE

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13
Q

this effects (?) the removal of components of water from double bond

A

DEHYDRATASE

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14
Q

transaminases and kinases are examples of?

A

TRANSFERASE

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15
Q

effects the addition of the components of water to a double bond

A

HYDRATASE

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16
Q

enzyme that catalyzes a hydrolysis reaction where the addition of H20 mol to a bond causes the bond to break

A

HYDROLASE

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16
Q

catalyzes the isomerization and converts it into a mol, isomeric with itself

A

ISOMERASE

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17
Q

these reactions are central to the process of digestion

A

HYDROLASE

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18
Q
  • transfer of an amino group between substrates
  • transfer of a phosphate group between substrates
A

TRANSFERASES

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19
Q

one reactant and one product and where isomerase are operative

A

ISOMERASE

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20
Q
  • hydrolysis of ester linkages in lipids
  • hydrolysis of amide linkages in proteins
  • hydrolysis of sugar–phosphate ester bonds in nucleic acids
  • hydrolysis of glycosidic bonds in carbohydrates
  • hydrolysis of phosphate–ester bonds
A

HYDROLASES

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21
Q

enzyme that catalyzes the bonding together of two mol in one w/ the participation of ATP

A

LIGASE / SYNTHETASE

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22
Q
  • removal of H2O from a substrate
  • removal of CO2 from a substrate
  • removal of NH3 from a substrate
  • addition of H2O to a substrate
A

LYASES

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23
Q

generally energetically unfavorable and require simultaneous input of energy obtained by hydrolysis reaction where ATP turns into ADP

A

LIGASE / SYNTHETASE

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24
Q
  • conversion of D isomer to L isomer,or vice versa
  • transfer of a functional group from one position to another in the same
    molecule
A

ISOMERASES

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25
Q
  • formation of new bond between two substrates, with participation of ATP
  • formation of new bond bet. a substrate and CO2, with participation of ATP
A

LIGASES

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25
Q
  • oxidases
  • reductases
  • dehydrogenases
A

OXIDOREDUCTASES

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25
Q
  • Transaminases
  • Kinases
A

TRANSFERASES

26
Q

TRUE / FALSE:
Enzymes are protein catalysts that increase the velocity of a chemical reaction, and are NOT consumed during the reaction

27
Q
  • Lipases
  • Proteases
  • Nucleases
  • Carbohydrases
  • phosphatases
A

HYDROLASES

28
Q

RNAs with catalytic activity are called _________ and are much less commonly encountered than protein catalysts

29
Q
  • dehydratases
  • decarboxylases
  • deaminases
  • hydratases
30
Q

Enzyme molecules contain a special pocket or cleft

A

active site

30
Q

how many percentage are active sites in the entire protein structure?

31
Q

Enzyme-catalyzed reactions are highly efficient, proceeding from 103–108 times faster than uncatalyzed reactions

A

Catalytic efficiency

31
Q
  • oxidation of a substrate
  • reduction of a substrate
  • introduction of double bond (oxidation) by formal removal of two H atoms from substrate, the H being accepted by a coenzyme
A

OXIDOREDUCTASES

32
Q

the reactant in an enzyme-catalysed reaction

33
Q
  • Racemases
  • Mutases
A

ISOMERASES

34
Q

contains amino acid side chains that participate in substrate binding and catalysis

A

active site

34
Q
  • Synthetases
  • Carboxylases
35
Q

The number of molecules of substrate converted to product per enzyme molecule per second

A

turnover number

35
Q

region of an enzyme where substrate molecules bind and undergo a chemical reaction

A

active site

36
Q

Enzymes are highly specific, interacting with one or a few substrates and catalyzing only one type of chemical reaction

A

SPECIFICITY

36
Q

residues that form temporary bonds with the substrate

A

binding site

37
Q

residues that catalyse a reaction of that substrate

A

catalytic site

37
Q

4 TYPES OF SPECIFICITY

A

ABSOLUTE
GROUP
LINKAGE
STEREOCHEMICAL

38
Q

type of specificity where enzyme will catalyze only one reaction

39
Q

intermediate reaction species that is formed when a substrate binds to the active site of an enzyme

A

Enzyme–substrate complex

40
Q

Catalase enzyme catalyzes only
Hydrogen peroxide (H2O2) to H2O and O2

41
Q

2 types of ESC or Models of enzyme activity

A

Lock and key model
Induced fit model

41
Q

type of specificity where the enzyme will act only on molecules that have a specific functional group, such as hydroxyl, amino, or phosphate groups

42
Q

Only substrates with a complementary geometry can be accommodated at such a site

A

Lock and key model

43
Q

what type of specificity is Carboxypeptidase?

44
Q

simplest type and a product of enzyme specificity

A

Lock and key model

45
Q

the enzyme will act on a particular type of chemical bond, irrespective of the rest of the molecular structure

46
Q

allows for small changes in the shape or geometry of the active site of an enzyme to accommodate a substrate

A

Induced fit model

47
Q

what type of specificity is Phosphatases?

48
Q

induced fit is a result of the enzyme’s flexibility; it adapts to accept the incoming substrate

A

Induced fit model

49
Q

coenzyme is permanently associated with the enzyme and returned to its original form

A

prosthetic group

50
Q

the enzyme will act on a particular stereoisomer. Chirality is inherent in an enzyme active site because amino acids are chiral compounds

A

STEREOCHEMICAL

51
Q

Apoenzyme + nonprotein moiety (cofactor) = ?

A

holoenzyme

52
Q

An L-amino acid oxidase will catalyze the oxidation of the L-form of an amino acid but not the D-form of the same amino acid

A

STEREOCHEMICAL

53
Q

FACTORS AFFECTING ENZYMATIC ACTIVITY

A

A. Substrate concentration
B. Temperature
C. pH
D. Enzyme concentration

54
Q

Enzymes can be divided into two general structural classes

A

SIMPLE
CONJUGATED

55
Q

an enzyme composed only of protein (amino acid chains)

A

SIMPLE ENZYME

55
Q

an enzyme that has a nonprotein part in addition to a protein part

A

CONJUGATED ENZYME

55
Q

refers to the active enzyme with its nonprotein component

A

holoenzyme

55
Q

inactive enzyme without its nonprotein moiety or the protein part of the conjugated enzyme

56
Q

If the nonprotein moiety is a metal ion such as Zn2+ or Fe2+

56
Q

a small organic molecule

57
Q

Coenzymes that only transiently associate with the enzyme

A

cosubstrates

ENZYMES (MOD 4) (5 decks)

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