Chapter 13 - Enzymes Flashcards

0
Q

these are rxn catalysts

A

enzymes

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1
Q

are all enzymes proteins?

A

yes

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2
Q

the greek word of enzyme means

A

in yeast

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3
Q

primary structure refers to

A

sequence of amino acids

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4
Q

secondary structure refers to

A

alpha helix

beta pleated sheets

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5
Q

tertiary structure is

A

folding/3D

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6
Q

kelan may quaternary ang protein?

A

> 1 polypeptid

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7
Q

substance acted upon

A

substrate

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8
Q

found in enzyme; where substrate reacts

A

active site

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9
Q

found in enzyme; for regulation, inhibition etc

A

allosteric site

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10
Q

same function with the enzyme but in different form

A

isoenzyme

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11
Q

how are isoenzymes differentiated

A

electrophersis
solubility
heat stability
chemical inhibition

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12
Q

isoenzymes are different in ______ structure and same in _______ structure

A

primary; tertiary

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13
Q

non-CHON necessary for enzymatic activity

A

cofactors

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14
Q

type of cofactors

A

coenzyme

activator

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15
Q

organic type of cofactors

A

coenzyme

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16
Q

inorganic type of cofactors

A

activators

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17
Q

examples of activators

A
Mg
Ca
Cl
Cu
Co
Fe
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18
Q

examples of coenzymes

A
biotin
NAD
thiamine
pyrophosphate 
lipoic acid
flavin
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19
Q

coenzyme bound tightly to enzyme

A

prosthetic group

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20
Q

enzyme portionbound to prosthetic group

A

apoenzyme

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21
Q

prosthetic group + apoenzyme

A

holoenzyme

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22
Q

inactive form of an enzyme

A

proenzyme

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23
Q

classification of enzymes

A
oxidoreductase
transferases
hydrolases
lyases
isomerases
ligases
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24
what is the first digit in a pn enzyme's code
classification of enzyme
25
what is the second digit in an enzyme's code
subclass
26
responsible for the nomenclature of enzymes
IUB-EC
27
standard name of enzymes can be
substrate + "ase" | reaction + "ase"
28
enzyme responsible for oxidation reduction
oxidoreductase
29
enzyme responsible for the transfer of shit i don't know what shit
transferase
30
enzyme responsible for hydrolysis
di ko alam eh
31
enzyme responsible for the removal of a group without hydrolysis
lyases
32
enzyme responsible for the interconversion of geometric npositional optical isomers
isomerase
33
enzyme responsible for the joining of two substrates
ligases
34
only example of a ligase
glutathione synthetase
35
two ways to allow product formation
giving more energy | using enzymes
36
energy required to raise all molecules in 1 mole of a compound at a certain temp to the transition state of the peak of energy
activation energy
37
types of specificity
absolute group bond stereoisometric
38
optimum pH for most enzymes
7.0-8.0
39
optimum temp for most enzymes
37 oC
40
at what pH does trypsin work
1.0
41
high temp ________ enzymes
denatures
42
low temp ________ enzymes
inactivates
43
for every _____ increase in temp, rxn is doubled
10 oC
44
this shows the relationship betweenvelocity and substrate conc
Michaelis-Menten constant
45
the maximum point in the Michaelis-Menten curve is also the
saturation point
46
the point kung saan no matter gaano kadaming enzyme ang ilagay there is no more reaksyon na mangyayari
saturation point jk di kosure kung ganyan ba un
47
types of inhibition
competitive noncompetitive uncompetitive
48
inhibitor binds direly to active site, reversible
competitive
49
inhibitor binds to a site other than thrpe active site
noncompetitive
50
when is noncompetitive inhibition irresversible
if damage is brought to the catalytic site
51
inhibitor binds to ES complex itself
uncompetitive
52
increased substrate in uncompetitive inhibition would _____ inhibition
worsen
53
the enzyme combines with only one substrate
absolute specificity
54
enzyme combines with all substrates contain a particular chemical group
group specific
55
enzymes combines to substrates with certain chemical bonds
bond specificity
56
enzymes that predominantly combine with only one optical isomer of a certain compound
stereoisometric specificity
57
the rxn rate is directly proportional to substrate conc.
first order kinetics
58
how is enzyme activity measured? thru:
increase in product formation decrease in substrate formation(conc ata hindi form) decrease in coenzyme formation increase in conc of altered shitshit
59
amount of enzyme that will catalyze the rxn if 1 micromole of substrate per minute under specified condition enzyme activity
IU (kung anuman un)
60
two methods of enzyme activity measurement
fixed time/endpoint | continuous monitoring/kinetic assay
61
how many times is absorbance read in fixed time/endpoint
once
62
what are the major enzymes
TMTM
63
minor enzymes
``` OCT POD GOD ALS LAP ```
64
the recommended (?) name of creatine kinase
ATP:creatine-N-phosphotransferase
65
size of CK
82000 da
66
CK is associated mainly with _______ generation
ATP
67
major tissue sources of CK
skel muscle heart brain
68
minor tissue sources of CK | LLPPS PG BTUK
``` lung liver pancreas prostate spleen placenta GIT bladder thyroid uterus kidney ```
69
isoenzyme of CK
CK-MB CK-MM CK-BB
70
which CK isoenzyme is fastest toward anode
CK-BB
71
most electronegative CK isoenzyme
CK-BB
72
isoenzyme rarely seen in serum, mainly found in brain
CK-BB
73
least concentration among the CK isoenzymes
CK-BB
74
which CK isoenzyme is a hybrid
CK-MB
75
CK isoenzyme found mainly in the heart
CK-MB
76
CK isoenzyme found mainly in the skeletal muscle
CK-MM
77
normal CK-MB conc in total CK
<6%
78
two atypical isoenzyme of CK
mitochondrial CK | macro CK
79
where does mitochondrial CK migrate
before CK-MM (before origin)
80
CK isoenzyme indicating severe illness
mitochondrial CK
81
CK detected in cases of malignant tumor and cardiac abnormality
mitochondrial CK
82
where does ,acro CK migrate to
between MM and MB
83
this isoenzyme is CK-MM complexed with IgG, some IgA or lipoprotein
macro CK
84
age-sex related isoenzyme of CK
macro CK
85
normal conc. of macro CK
.8-1.6%
86
methods of CK isoenzyme measurement
electrophoresis ion exchange chromatography immunoassays double antibody inhibition
87
what is visualized in electrophoresis of CK that is cathodal to CK-MM
AK (kung ano man yan)
88
immunoassay of CK isoenzymes use antibodies against ____________
H and B subunit
89
methods of CK det
Tanzer-Gilvarg | Oliver Rosalki
90
optimum pH of Tanzer Gilvarg
9.0
91
CK det method coupled w/ PK-LD-NADH system
Tanzer Gilvarg
92
forward type of CK det method
Tanzer Gilvarg
93
optimum pH of Oliver Rosalki
6.8
94
Ck det method coupled w/ HK-G6PD-NADP system
Oliver Rosalki
95
which is faster? Tanzer Gilvarg or Oliver Rosalki?
Oliver Rosalki
96
ref range of CK in males
15-160 U/L
97
CK-MB conc of >6% indicates
myocardial infarction
98
ref range of CK in females
15-130 U/L
99
instability of CK is resolved with
sulfhydryl compounds
100
example of sulfhydryl compounds
dithiothreitol | thioglycerol
101
does light inactivate CK
yes
102
higher CK values in men are attributed to incresed
muscle mass
103
enzyme responsible for interconversion of lactic and pyruvic acid
lactate dehydrogenase
104
how does LD work
transfer H+ using coenzyme NAD+
105
major tissue source of LD
heart liver skel muscle erythrocytes
106
minor tissue sources of LD
lung | smooth muscle
107
diagnostic significance of LD
``` cardiac hepatic skel disease renal pernicious anemia ```
108
isoenzymes of LD
LD1 - LD6
109
fastest LD isoenzyme
LD1
110
highest conc among LD isoenzyme
LD2
111
highest affinity to anode LD isoenzyme
LD1
112
an LD idornzyme that is a bad prognosis and indicates impending death
LD6
113
order of LD isoenzymes most con to lowest conc
2 > 3 > 1 > 4 > 5
114
an atypical LD isoenzyme
macro LD
115
found between LD3 and LD4
macro LD
116
LD1 conc higher than LD2 indicates
myocardial infection
117
highest affinity LD isoenzyme to anode
LD1
118
methods for LD measurement
Wacker | Wroblewski La Due
119
endpoint of Wacker method
blue purple color
120
mol weight of LD
128000 da
121
LD6 is called
alcohol dehydrogenase
122
which LD measurement methd is forward
Wacker
123
by how many tomes is Wroblewski La Due faster than Wacker
3x
124
other name for AST
serum glutamic oxaloacetatic transaminase
125
major tissue sources of AST
cardiac muscle skel muscle liver
126
minor tissue sources of AST
kidney pancreas RBCs
127
methods for AST det
Reitman-Frankel | coupling with diazonium salts
128
mechanism of Reitman-Feankel
ketoacids is reacted to 2,4-dinitrophenylhydrazine (DNPH)
129
product of Reitman-Frankel
ketoacid hydrazones
130
falsely decreases AST level
mercury cyanide fluoride
131
example of liver diseases
viral hepatitis | cirrhosis
132
is AST useful in diagnosis of AMI
hindi eh
133
example of skeletal muscle disorder
muscular dystrophies
134
the optimum pH for Karmen method
7.3-7.8
135
absorbance of AST Karmen method
340nm
136
AST activity is stable in serum for ______ days at ref temp
3-4 days
137
catalyzes transfer of an amino group from alanine to alpha ketoglutarate wih the formation of glutamate and pyruvate
alanine aminotransferase
138
old term for ALT
serum glutamic pyruvic transaminase
139
major tissue source of ALT
liver | cardiac tissue
140
diagnostic significance of ALT
hepatic parenchymal disease AMI or heart failure IM muscular dystrophy
141
most labile LD isoenzyme
LD5
142
LD activity in serum is _______
unstable
143
how is sample for LD stored
25 oC
144
gaano katagal dapat matest ang LD
within 48hrs
145
gaano katagal dapat matest ang LD isoenzyme
24hrs
146
ref range of LD
125-220 U/L
147
half life of ALT
24hrs
148
indicator enzyme for ALT assay
LD
149
absorbance for ALT
340nm
150
methods for ALT measurement
Karmen Reitman coupling w/ diazonium salt
151
unaffected by hemolysis
ALT
152
stability of ALT
3-4days at 4 oC
153
ref range for ALT
6-37 U/L
154
catalyzes hydrolysis of various phosphomonoesters at an alkaline pH
alkaline phosphatase
155
coenzyme for ALP
pyridoxal phosphate
156
activator for ALP
Mn | Mg
157
optimal pH for ALP
9.0-10.0
158
major tissue source of ALP
``` intestine liver bone spleen placenta kidney ```
159
ALP isoenzymes
liver ALP bone ALP placenta ALP intestinal ALP
160
diagnostic significance of ALP
hepatobiliary | bone disorders
161
in bone disorders, there is elevation in ALP when ____ are involved
osteoblast
162
example of bone disorder where ALP is elevated
Paget's disease
163
which ALP isoenzyme migrates the fastest
liver ALP
164
liver is further divided into
major liver band | fast or alpha 1
165
who are most likely to possess intestine ALP
blood type B and O | secretors
166
ALP isoenzyme differentiation
electrophoresis heat stability chemical inhibition
167
order of ALP isoenzymes in electrophoresis
fast > major > Regan Nagao > bone > placenta > intestinal
168
which ALP isoenzyme resust denaturation at 65 oC for 30 minutes
placental ALP
169
atypical ALP isoenzyme
Regan Nagao
170
other name for Regan Nagao
carcinoplacental ALP
171
ectopic product of an enzyme by malignant tissue
Regan isoenzyme
172
may be considered a variant of Regan isoenzyme
Nagao
173
what inhibits Nagao
L-leucine
174
which best inhibits intestinal and placentaL ALP
phenylalanine
175
detected in metastatic carcinoma and adenocarcinoma
Nagao
176
mechanism of Bowers McComb (ALP)
p-nitrophenylphosphate -> p-nitrophenol + phosphate ion
177
absorbance sa Bowers McComb
405nm
178
high fat meals _______ ALP
increase by 25%
179
ref range of ALP
30-90 U/L
180
optimal pH for ACP
5.0
181
tests for ALP
``` Bodansky King-Armstrong or Cutman Gutman Bessey-Lowry-Brock Hudson Babson Reed Bowers McComb Sinowara Jones Reinhart ```
182
basic difference in ALP and ACP
pH
183
major tissue source of ACP
prostate
184
minor source of ACP
``` bone liver spleen kidney erythrocytes platelets ```
185
diagnostic significance of ACP
hyperplasia of prostate rape cases bone disease heart cancer prostatic carcinoma metastatic carcinoma
186
most specific substrate for prostatic ACP
thymolphthalein monophosphate
187
chemical inhibition of prostatic ACP usually uses ____ as inhibitor
tartrate
188
formula for pACP
total ACP - ACP after tartrate inhibition
189
PSA stands for
prostate-specific antibody
190
inhibitor for non-pACP
copper
191
serum activity _____ within _______ if the sample is left at rm tmp unpreserved
decrease; 1-2hrs
192
ref range for ACP
0-35 ng/mL
193
upon clotting, serum for ACP det must be
separated immediately