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MedBiochem > quiz 1.3 enzymes to metab > Flashcards

quiz 1.3 enzymes to metab Flashcards

1
Q

conponents of holoenzyme

A

apoenzyme

cofactor

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2
Q

name ng compelte na enzyme

A

holoenzyme

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3
Q

organic cofactors can be ____ ______

A

prosthetic

2nd subtrate

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4
Q

inorganic cofactors may be ____ ____

A

metallo enzyme

ion activators

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5
Q

are cofactors heat stable or labile?

A

stable

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6
Q

mechanism of action of cofactors

A

transfer and/or accept functional groups

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7
Q

at the end of the rxn, coenzymes _______

A

revert to orig state

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8
Q

coenzymes mostly derived from

A

vitamins

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9
Q

NAD is derived from

A

nicotinic acid

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10
Q

LIPOIC ACID is derived from

A

none

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11
Q

pyridoxal phosphate is derived from

A

pyridoxine vit b5

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12
Q

biochtin is derived from

A

biotin

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13
Q

coenzymes not derived from vits

A

cenzyme q
tetrahydrobioprotein
lipoic acid

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14
Q

classif of coenzymes

A

thos that tranfer H

those that transfer pther than H

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15
Q

where is the active site of NAD

A

C4 or pyridine ring

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16
Q

rxns involving NAD conezyme

A

LDH

malaye dehydrogenase

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17
Q

rxns using NADP

A 
G6PD
reductive biosynthesis (NADPH)
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18
Q

conezyme to succinic acid dehydrogenase is tightly bound thru

A

histidine

end product: fumaric acid

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19
Q

rxns using FAD

A

succinic acid dehydr
fatty acylCoA
l-amino acid oxidase (FMN)

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20
Q

absorbance for FAD/FADH2 and ano itsura

A

450nm
FAD intense color
FADH2 colorless

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21
Q

the ubiquitous coenzyme

A

ubiquinone

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22
Q

structure of uniquinone

A

has benzoquinone with side chains of repeating isoprenoid unis

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23
Q

active sites of uniquinone

A

C1 and 4

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24
Q

rxn where may ubiquinone

A

etc

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25
Q

absorbance ng ubiquinone and ano itsura

A

270-290nm

oxidized form absorbs but disappears when reduced to hudroquinone form

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26
Q

conezyme fo the aromatic amino acids

A

tetrahydrobiopterin

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27
Q

thiamine pyrophosphate is derived from

A

thiamine B1

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28
Q

structure ng TPP

A

subsituted pyrimidine linked to thiazole ring with terminal phosphate

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29
Q

TTP requires

A

Mg++

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30
Q

TPP is ainactivated by

A

thiaminase found in raw fish

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31
Q

rxns using TPP

A 
puruvic decarboxylase (nonoxid)
pyruvic dehydrogenase (oxid)
transkeolase
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32
Q

active site ng TPP

A

C2 ng thiazole ring

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33
Q

rxns using tetrahydrobiopterin

A

phenylalanine hydroxylase

tryptophan hydroxylase

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34
Q

action of TPP

A

transfers binds aldehyde and ketol groups thru its carbanion center

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35
Q

2 forms of lipoic acid

A

cyclic/oxidized

open:reduced

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36
Q

action of lipoic acid

A

sulfur group accepts and transfers acyl groups and H+

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37
Q

coenzyme A is derived from

A

pantothenic acid

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38
Q

active site g coenzyme A

A

ung sulfur sa dulo kung saan man un

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39
Q

structure ng bicytin

A

imidazolone ring fused with tetrahydrothiophene linked with valeric acid

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40
Q

biocytin is inactivated by

A

avidin in raw egg white

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41
Q

biocytin is derived from

A

nbiotin

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42
Q

mechanism or action ng biotin

A

carboxylation

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43
Q

ano ung mga may lysine na coenzyme

A

biocytin

lipoic acid

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44
Q

rxns using biocytin

A

acetyl CoA carboxylase
pyruvate carbyxolase
propionyl carboxylase
methylmalonyl CoA carboxylase

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45
Q

2forms of pyridoxal phosphate

A

pyridoxal phosphate

pyridoxamine phosphate

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46
Q

active site ng pyridoxal phosphate

A

aldehyde group at C4

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47
Q

pyridoxal phosphate reacts with alpha amino of amino acid substrate to form

A

schiff’s base

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48
Q

three rxns that lyridoxal phosphate uses

A

transamination
decarboxation
racemization

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49
Q

pyridoxal phosphate is k inhibited by

A

isoniazid (INH) antiTb drug

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50
Q

pyridoxal phosphate binds to what of enzyme

A

lysine

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51
Q

how is schiff’s base formed

A

pyridoxal bla reacts with alpha amino of amino acid substrate

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52
Q

rxns using pyridoxal bla

A

ALT AST
amino acid decarbo
amino acid racemase

53
Q

transaminase mechanism

A

pyrudoxal bla > aldimine > ketimine > puridoxamine

54
Q

me hanism where intermediate products are released even before all substrate added

A

ping pong

55
Q

structure ng tetrahydro flouc acid

A

pterin rin linked to p-aminobenzoic acid bound to glutamic

56
Q

avtive sites ng terragydrofolic nla

A

N5 ng pterin ring

N10 ng PABA

57
Q

conezyme inhibited by

A

folate antagonists

like methotrexate and sulfonamides

58
Q

rxns using tetrahydrofolate

A

serine hydroxymethyl transferase
thumidile synthetase
formyl synthetase

59
Q

rxns that cobamide coenz use

A

racmization:isomerization

transmethylation

60
Q

2forms ng cobamide coenz

A

deoxyadenosyl conalamin

methylcobalamin

61
Q

rxns using cobamide coenz

A

methylmalonyl CoA mutase

methionine synthase

62
Q

active sites of FAD/FMN

A

N1 and 5

63
Q

special com[onent of FAD/FMN

A

isoalloxazine ring

64
Q

the coenzyme used in ETC

A

ubiquinone

65
Q

a rxn using coenzyme A that activates palmitic acid for use

A

fatty acyl CoASH synthase

66
Q

class 1 enzyme

A

oxidoreductases

67
Q

class 2 enzyme

A

transferases

68
Q

class 3 enzymes

A

hydrolases

69
Q

class 4 enzymes

A

lyases

70
Q

class 5 enzymes

A

isomerases

71
Q

class 6 enzymes

A

ligases

72
Q

refers to the protein part of the enzyme

A

apoenzyme

73
Q

refers to the nonprotein part of the enzyme

A

cofactor/prosthetic group

74
Q

the complete active enzyme is called

A

holoenzyme

75
Q

in transferases, generally, the addition of _____ stimulates activity of receptor

A

phosphate

76
Q

this is the regulation of attachment of whatever bla di ko na-note

A

covalent modification

77
Q

what is the action of hydrolases

A

addition of water to break bonds

78
Q

enzymes that are present at a constant amount in the cell

A

constitutive/housekeeping

79
Q

enzymes that is induced by a particular substrate (genetic control)

A

inducible

80
Q

model that states the binding site contains amino acid residues rearranged in complementary 3D surface which bind the substrate through various interactions

A

rigid tempate model (lokc and key)

81
Q

who formulated lock and key model of active sites

A

fischer

82
Q

who formulated the induced fit model of active sites

A

koshland

83
Q

model that states that as the substrate binds, te enzyme undergoes a conformational change which positions the side chains of the amino acids in the active site and increases the number of boinding interactions

A

induced fit model

84
Q

two perspectives that explain the action of enzymes

A

thermodynamic changes

processes at the active site

85
Q

difference in free energy between transition and substrate is called

A

Gibbs free energy of activation

86
Q

diff. processes at the active site

A 
proximity/orientation effect
desolvation effect
acid base catalysis
covalent catalysis
strain effect
metal coordination effect
87
Q

the reacting groups are close enough or properly oriented as to favor formation of products

A

orientation/proximity effects

88
Q

removal of water molecules accelerate enzymatic rxns

A

desolvation effects

89
Q

removal of _______ accelerates enzymatic rxns

A

water

90
Q

amino acid side chains on the enzyme acts as both proton acceptor and donor

A

acid base catalysis

91
Q

covalent catalysis is aka

A

nucleophilic catalysis

92
Q

nucelophilic side chains of amino acids on enzyme attacks nucleophilic parts of substrate and form covalent bonds

A

covalent catalysis/nucleophilic catalysis

93
Q

conformational change subsequent to substerate binding may lead to distortion on some parts of the substrate

A

bond distortion/strain effects

94
Q

etal ions acts as lewis acids which can accept electron pair to form a sigma bond

A

metal coordination effects

95
Q

metalloenzymes are ______ bound

A

tightly

96
Q

metal-activated enzymes are _____ bound

A

loosely

97
Q

________________ always present cofactor metal ion

A

magnesium

98
Q

the plot of pH vs. enzyme activity and temp vs activity gives a _____ shape

A

bell

ps. optimum pH and temp at peak

99
Q

the enzymes are ______ beyond optimal pH and high temps

A

denatured

100
Q

enzyme activity _______ proportionately to the conc. of th enzyme

A

increases

101
Q

substrate concentration is shown in what graph

A

Michaelis Menten saturation graph

102
Q

as subs. conc. increases, velocity increase only to a point when _________

A

enzyme is saturated with the substrate

103
Q

a _____________ is obtained when activity of enzyme is plotted against substrate conc.

A

rectangular hyperbola

104
Q

vmax _____ and km ______ with competitive inhibitors

A

normal; inc

105
Q

vmax _____ and km ______ with noncompetitive inhibitors

A

dec; same

106
Q

vmax _____ and km _____ with uncompetitive inhibitors

A

dec; dec

107
Q

amount of activity that catalyzes the transformation of 1 umol of substrate per minute under specified conditions

A

IU

108
Q

number of enzyme units per milligram of protein

A

specific activity

109
Q

units of enzyme activity per umol pf enzyme

A

turnover rate or catalytic constant (kcat)

110
Q

amount of enzyme activity that transform 1 mole of substrate per second

A

katal(kat)

111
Q

specific rate constants of the reversible rxn

A

ks

112
Q

ther eciprocal of the michaelis menten

A

lineweaver burke

113
Q

slope in the lineweaver burke

A

km/vmax

114
Q

is defined as the substrate concentration at 1/2 the maximum velocity

A

km

115
Q

allosteric enzymes give _____ curves of V vs S

A

sigmoidal shaped

116
Q

the concerted kung anuman to is aka

A

Monod-Wyman-Chageux

117
Q

the sequential kung anuman to is aka

A

koshland-Nemethy-Filmer

118
Q

model that describes allosteric transitions of proteins made up of identical subunits

A

Monod-Wyman-Chageux

119
Q

This model of allosteric regulation holds that subunits are not connected in such a way that a conformational change in one induces a similar change in the others.

A

koshland-Nemethy-Filmer

120
Q

binding of one ligand to one protomer can affect the binding of the same ligand to another protomer

A

homotropic interactiond

121
Q

binding of one ligand affects the binding of a different ligand to another protomer

A

heterotropic interactions

122
Q

means of enzyme regulation

A

allosteric effectors
reversible covalent modif.
stimulation and inhibition of control protein
proteolytic activation

123
Q

inactive precursors of enzymes are called

A

zymogen/ptoenzymes

124
Q

intracellular signaling that involves two mechanism

A

juxtacrine signaling

125
Q

the two emchanism in juxtacrine signaling

A

gap juntion channels

interaction of proteins expressed on the serface of sender cell

126
Q

signal transduction that involves hormones secreted and long distance transport to target cells

A

endocrine signaling

127
Q

transduction taht involves molecules secreted into its immediate or local environment

A

paracrine

128
Q

a signaling specific to neurons

A

synaptic or neuronal signaling

MedBiochem (16 decks)

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