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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
* removal of H2O from a substrate * removal of CO2 from a substrate * removal of NH3 from a substrate * addition of H2O to a substrate
LYASES
23
generally energetically unfavorable and require simultaneous input of energy obtained by hydrolysis reaction where ATP turns into ADP
LIGASE / SYNTHETASE
24
* conversion of D isomer to L isomer,or vice versa * transfer of a functional group from one position to another in the same molecule
ISOMERASES
25
* formation of new bond between two substrates, with participation of ATP * formation of new bond bet. a substrate and CO2, with participation of ATP
LIGASES
25
* oxidases * reductases * dehydrogenases
OXIDOREDUCTASES
25
* Transaminases * Kinases
TRANSFERASES
26
TRUE / FALSE: Enzymes are protein catalysts that increase the velocity of a chemical reaction, and are NOT consumed during the reaction
TRUE
27
* Lipases * Proteases * Nucleases * Carbohydrases * phosphatases
HYDROLASES
28
RNAs with catalytic activity are called _________ and are much less commonly encountered than protein catalysts
ribozymes
29
* dehydratases * decarboxylases * deaminases * hydratases
LYASES
30
Enzyme molecules contain a special pocket or cleft
active site
30
how many percentage are active sites in the entire protein structure?
10 - 20%
31
Enzyme-catalyzed reactions are highly efficient, proceeding from 103–108 times faster than uncatalyzed reactions
Catalytic efficiency
31
* 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
OXIDOREDUCTASES
32
the reactant in an enzyme-catalysed reaction
substrate
33
* Racemases * Mutases
ISOMERASES
34
contains amino acid side chains that participate in substrate binding and catalysis
active site
34
* Synthetases * Carboxylases
LIGASES
35
The number of molecules of substrate converted to product per enzyme molecule per second
turnover number
35
region of an enzyme where substrate molecules bind and undergo a chemical reaction
active site
36
Enzymes are highly specific, interacting with one or a few substrates and catalyzing only one type of chemical reaction
SPECIFICITY
36
residues that form temporary bonds with the substrate
binding site
37
residues that catalyse a reaction of that substrate
catalytic site
37
4 TYPES OF SPECIFICITY
ABSOLUTE GROUP LINKAGE STEREOCHEMICAL
38
type of specificity where enzyme will catalyze only one reaction
ABSOLUTE
39
intermediate reaction species that is formed when a substrate binds to the active site of an enzyme
Enzyme–substrate complex
40
Catalase enzyme catalyzes only Hydrogen peroxide (H2O2) to H2O and O2
ABSOLUTE
41
2 types of ESC or Models of enzyme activity
Lock and key model Induced fit model
41
type of specificity where the enzyme will act only on molecules that have a specific functional group, such as hydroxyl, amino, or phosphate groups
GROUP
42
Only substrates with a complementary geometry can be accommodated at such a site
Lock and key model
43
what type of specificity is Carboxypeptidase?
GROUP
44
simplest type and a product of enzyme specificity
Lock and key model
45
the enzyme will act on a particular type of chemical bond, irrespective of the rest of the molecular structure
LINKAGE
46
allows for small changes in the shape or geometry of the active site of an enzyme to accommodate a substrate
Induced fit model
47
what type of specificity is Phosphatases?
LINKAGE
48
induced fit is a result of the enzyme’s flexibility; it adapts to accept the incoming substrate
Induced fit model
49
coenzyme is permanently associated with the enzyme and returned to its original form
prosthetic group
50
the enzyme will act on a particular stereoisomer. Chirality is inherent in an enzyme active site because amino acids are chiral compounds
STEREOCHEMICAL
51
Apoenzyme + nonprotein moiety (cofactor) = ?
holoenzyme
52
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
STEREOCHEMICAL
53
FACTORS AFFECTING ENZYMATIC ACTIVITY
A. Substrate concentration B. Temperature C. pH D. Enzyme concentration
54
Enzymes can be divided into two general structural classes
SIMPLE CONJUGATED
55
an enzyme composed only of protein (amino acid chains)
SIMPLE ENZYME
55
an enzyme that has a nonprotein part in addition to a protein part
CONJUGATED ENZYME
55
refers to the active enzyme with its nonprotein component
holoenzyme
55
inactive enzyme without its nonprotein moiety or the protein part of the conjugated enzyme
apoenzyme
56
If the nonprotein moiety is a metal ion such as Zn2+ or Fe2+
COFACTOR
56
a small organic molecule
COENZYME
57
Coenzymes that only transiently associate with the enzyme
cosubstrates

ENZYMES (MOD 4) (5 decks)

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