Unit 2 Flashcards
(240 cards)
1
Q
The 3-D conformation is able to fulfill a specific ________
A
Biologic function
2
Q
The 3-D structure is also known as the _______ ______ that has a large number of favorable interactions within the protein
A
Native fold
3
Q
There is a cost in _________ ________ of folding the protein into one specific native fold
A
Cost in conformational entropy
4
Q
What are the favorable interactions in proteins?
A
Hydropphobic effect
Hydrogen bonds
London dispersion (Van der Waals)
Electrostatic interactions
5
Q
The resonance causes the peptide bonds
- to be _______ reactive compared to esters
- to be quite ______ and nearly ______
- to exhibit a large ________ _____ in the favored trans configuration
A
Less reactive
Rigid and nearly planar
Dipole moment
6
Q
What type of linkages are seen in primary structures?
A
Covalent
7
Q
Secondary structures contain what linkages and structures?
A
H-bonds
Alpha helices, beta sheets and beta turns
8
Q
In the tertiary structure, what linkages are involved? And what are the linkages between?
A
Covalent
H-bond
Van der Waals
And hydrophobic
Linkages between the R groups
9
Q
What is a peptide bond?
A
A bond formed by the carbonyl group and the amide group of another molecule
10
Q
Quaternary structures contain all types of linkages except _______
A
Covalent
11
Q
Where are the molecules bonded in quaternary structure?
A
Between subunits (mostly using R groups)
12
Q
Virtually all peptide bonds in proteins occur in ______ configuration
A
Trans
13
Q
What constitutes the polypeptide backbone?
A
The bond between the N and carbonyl carbon
14
Q
The alpha helix is stabilized by H bonds between ________
A
Nearby residues
15
Q
The beta sheet is stabilized by H-bonds between ________
A
Adjacent segments that may not be nearby
16
Q
Irregular arrangement of the polypeptide chain is called the ________ _____
A
Random coil
17
Q
Where does trypsin cleave at?
A
Lysine and arginine
18
Q
Cyanogen bromide cleaves at ______
A
Methionine
19
Q
Is the alpha helix right handed or left handed?
A
Right handed with 3.6 residues per turn
20
Q
Peptide bonds are aligned roughly ______ with the helical axis
Side chains point out and are roughly_____ with the helical axis
A
Parallel
Perpendicular
21
Q
What are strong helix formers? And what are some examples?
A
Small hydrophobic residues such as Alanine and Leucine are strong helix formers
22
Q
What acts as a helix breaker and why?
A
Proline acts as a helix breaker because the rotation around the N-Ca bond is impossible
Glycine acts as a helix breaker because the R-group supports of conformations
23
Q
What affects the formation of a helix?
A
Attractive or repulsive interactions etween side chains 3-4 amino acids apart
24
Q
What is the functional insulin part?
A
C-peptide
25
In ______ ____, release of water molecules from the structured solvation layer around the molecule as protein folds increases the net entropy
Hydrophobic effect
26
What are the favorable interactions in proteins?
Hydrophobic effect
H bonds
London dispersion
Electrostatic interactions
27
What are the hallmark features of primary structure of proteins?
```
Covalent bonds (peptide bonds)
Made up of amino acid chains
```
28
What are the characteristics of secondary structures of proteins
H-bonds between peptide bonds
Types: alpha helix, beta sheets, beta turn
29
What is characteristic of tertiary proteins in terms of linkages
Covalent, H-bond, ionic, van der Waals and hydrophobic
Stability and linkages are formed based on the R groups
30
What are the types of tertiary structure?
Super-secondary structures such as motifs and domains
31
What is characteristic of quaternary structure?
All types of linkages except covalent
| And interactions that form a quaternary structure is between subunits
32
What are types of quaternary structure?
Dimers and tetramers etc.
33
Structure of the protein is partially dictated by the properties of the ______ ______
Peptide bond
34
The ____ ______ is a resonance hybrid of two canonical structures
Peptide bond
35
The resonance causes the peptide bonds to be what 3 things?
Less reactive compared to esters
Rigid and nearly planar
Exhibit a large dipole moment in the favored trans configuration
36
What bond constitutes the polypeptide backbone?
N and alpha carbon carbonyl
37
What are the 5 functions of globular proteins?
```
Storage of ions and molecules
Transport of ions and molecules
Defense against pathogens
Muscle contraction
Biological catalysis
```
38
What globular proteins function in storage of ions and molecules?
Myoglobin and ferritin
39
What globular proteins function to transport ions and molecules?
Hemoglobin and serotonin transporter
40
What globular proteins funciton in defense against pathogens
Abs and cytokines
41
What are examples of globular proteins that function in muscle contraction?
Actin and myosin
42
What are some examples of globular proteins that function in biological catalysis?
Chymotrypsin and lysozyme
43
A molecule that binds to a protein is called a _______
Ligand
44
A region in the protein where the ligand binds is called the _______ _____
Binding site
45
Ligand binds via same ________ forces that dictate protein structure
Noncovalent
46
What allows the interactions of globular proteins with other molecules to be transient?
Ligands binds via noncovalent forces
47
What is the kinetics process?
The association rate constant Ka or the dissociation constant Kd
48
How do you know the Ligand and protein binding have reached equillibrium?
When the association and dissociation rates are equal
49
The ______ _______ is characterized by the equillibrium constant Ka
Equillibrium constant
50
What does Kd equal?
The concentration of ligand at which half of the available ligand-binding sites are occupied
51
If Kd is low, the binding affinity is _______
Tight
52
The lower the binding constant, the ________ the affinity
Higher
53
______ is the main oxygen storage protein
Myoglobin
54
______ is a circulating oxygen binding protein
Hemoglobin
55
The lower the affinity, the ______ the Kd value
Higher
56
Some transition metals bind O2 well but would generate _____ _______ if free in solution
Free radicals
57
Only _________ of Fe can be bound to myoglobin
Fe2+
58
_________ is free heme that is not bound to myoglobin
Fe3+
59
What are the components of heme?
Organic component: Protoporphyrin IX
| Inorganic component: Iron (Fe2+)
60
How many coordination bonding sites are on the Heme-Fe?
4 bonded to the nitrogen atoms of the protoporphyrinIX and 2 perpendicular to the plane of the ring
61
The perpendicular sites on the heme are made up of what?
His residue on the proximal side
| Oxygen binding site on the distal side
62
_________, ___, is the typical globular protein with most nonpolar a.a. Inside (except for the 2 Histidines which bind ______ and ______
Myoglobin, Mb,
Fe and O2
63
Where is myoglobin typically located?
Heart, muscle and liver
64
Binding to O2 is _______, it only depends on the [Mb] and on the pO2
Simple
65
Myoglobin has _____ helices terminate by _____ or Beta turns and loops
8
| Proline
66
Fe3+ or the ferric state is also known as _________, and Oxygen cannot bind to it
Metmoglobin
67
The iron ion in the ferric state (or metmoglobin) _________ bind to oxygen
Doesn’t
68
______ blocks funciton of myoglobin, hemoglobin and mitochondrial cytochromes that are involved with oxidative phosphorylation
Carbon monoxide
69
Which has a higher affinity for hemeoglobin, oxygen or carbon monoxide?
Carbon monoxide
70
Why cant myoglobin transport O2?
Because it would not release the oxygen to the tissues because of its high affinity
71
______ is a tetrameric protein of 2 identical globin subunits
Hemoglobin
72
What makes up hemoglobin?
2 alpha globins and 2 beta globins and each globin molecules is structurally similar and folds like myoglobin
73
In hemoglobin, each globin molecule has a ______ group
Heme
74
Interactions in hemoglobin between the alpha and beta globins is _____ than interactions between the 2alphabbeta dimers
Stronger
75
What is the difference between myoglobin and hemoglobin’s oxygen saturation curve?
Myoglobin saturation curve is more hyperbolic meaning it has a higher affinity for myoglobin.
Hemoglobin saturation curve is more S shaped to where it has high affinity but not as strong as myoglobin
76
_______ binds too tightly to be useful in O2 transport
Mb
77
______ binds O2 cooperatively
Hb
78
Binding of O2 at heme-Hb site ________ the likelihood that O2 binds ar the remaining unoccupied sites and vice versa
Increases
79
What is the make up of hemoglobin?
2 alpha globulins and 2 beta globulins
Each has a heme group and behaves like a protein made of 2 identical dimers (alphaBeta)2
80
The interaction between the alpha and beta globins is mostly _________. The interaction between the alphabeta dimers is mostly ________
Hydrophobic
Ionic
81
Hb is mainly a transporter protein for ____ but it also binds and transports ______
O2
CO2
82
Adult Hb is identified as ______
| Fetal Hb is identified as __________
HbA (alphabeta)2
HbF (alphagamma)2
83
Hb__ binds with greater affinity to O2 than Hb___ does
HbF; HbA
84
What are the two states of Hb?
Relaxed and tense state
85
O2 binding triggers a conformational change from the _____ state to the _____ state
T-state-> R state
86
Conformational change from the T state to the R state involves what?
Breaking ion pairs between the alpha1-Beta-2 interface
87
What triggers the conformational change from T to R state?
The binding of O2 to the histidine residue
| Slide 28
88
Conformation change from the T state to the R state involves breaking what?
Breaking ion pairs between the alpha1 and beta 2 interface
89
The pH difference between the lungs and metabolic tissues _______ efficiency of the O2 transport
Increases
90
What is the Bohr effect?
The pH difference between lungs and metabolic tissues increases efficiency of the O2 transport
91
H+ binds to Hb and stabilizes the _____ state of Hb
T state
92
Explain how H+ binding to Hb stabilizes the T state
Protonates His146 which then forms a sal bridge with Asp94 -> leads to the release of O2 in the tissues
93
At a higher pH O2 has a _______ affinity for Hb
| At a lower pH O2 has a ______ affinity for Hb
Higher
| Lower
94
_______ forms additional salt bridges stabilizing the T state
Carbamate
95
CO2 is exported out of the peripheral tissues as what 3 forms?
Carbamate on the amino terminal residues of each polypeptide subunits
Bound to Heme as CO2
Exported as dissolved bicarbonate
96
CO2 conversion to bicarbonate produces _____ leading to a ______ in pH
Proton; decrease
97
What promotes the release of O2 from Hb in peripheral tissues?
Protons and CO2
98
What form of Hb does lower pH and higher CO2 stabilize?
The T state of Hb facilitating the release of bound oxygen
99
What is another name for the R form of Hb?
Oxyhemoglobin
100
Oxyhemoglobin (R form) prevails in the ______
Lungs
101
```
The R form or oxyhemoglobin form prevails when (high or low):
PO2 ______
PCO2______
[H+] _____
pH ______
[BPG] ______
```
```
pO2 high
pCO2 low
[H+] low
pH high
[BPG] low
```
102
What is another name for the T form of Hb?
Deoxyhemoglobin
103
Where does the Deoxyhemoglobin (T form) prevail at in the body?
The peripheral tissues
104
```
The deoxyhemoglobin (T-form) prevails when the following are high or low?
pO2 ______
pCO2 ____
[H+]_____
pH _____
[BPG] _____
```
```
pO2 low
pCO2 high
[H+] high
pH low
[BPG] high
```
105
What is an example fo a negative heterotropic regulator of Hb function
2,3 Bisphosphoglycerate (2,3 BPG)
106
What Small negatively charged molecule binds to the positively charge central cavity of Hb and stabilizes the T state?
2,3 BPG
107
Why is 2,3 BPG important in erythrocytes?
Without 2,3 BPG Hb would be extremely inefficient in transporting O2 releasing only 8% of its cargo in the tissues
108
2,3 BPG is a(n) ________ ______ because biding to Hb affects its binding to O2
Allosteric regulator
109
2,3 BPG binds mostly to ______ amino acids in the Bet globins in the center of the tetramer of Hb. This pocket is only present in the ____ form of Hb
Basic
| T form
110
On the T-to-R transition what happens to 2,3 BPG
The pocket where 2,3 BPG binds collapses and 2,3BPG is released
111
In order for the structural transition from T to R to take place what must happen to the bonds between Hb and 2,3 BPG?
They must be broken
112
What has a higher oxygen-binding affinity, HbF (fetal Hb) or HbA (adult Hb)?
HbF
113
What amino acid exchange goes on leading to the sickle cell shape of RBCs in sickle cell anemia?
Valine replaces glutamic acid
114
How does the exchange of glutamic acid for valine in th beta chain of Hb result in sickle cell?
Glutamic acid is a hydrophilic amino acid while valine is a hydrophobic branched chain amino acid. The different properties of these amino acids results in a change from the biconcave disc to a sickled cell shape
115
Imbalance in production of Hb chains results in ________
Thalassemias
116
What happens in alpha-thalassemia?
Alpha globins are not produced in sufficient amounts
Some Hb contains only the beta globins that bind to O2 highly with very poor release of O2
117
What happens in beta thalassemia?
Beta globins are not produced in sufficient amounts
Alpha globins form aggregates that precipitate inside immature RBC producing anemia
118
What small protein is found in RBC that binds to alpha chains and keeps them properly folded and in solution?
AHSP (alpha-hemoglobin stabilizing protein)
119
Muscle contraction occurs through a series of conformational changes to protein structure due to what 3 things?
Binding
Hydrolysis
Release of ATP and ADP
120
What are the four steps to the actomyosin cycle?
1) ATP binds to myosin -> myosin dissociates from actin
2) ATP is hydrolyzed -> conformational change of myosin
3) myosin reconnects tot he actin filament at a different location -> release of Pi
4) release of Pi-> power stroke where myosin returns to initial state; shifting actin filament relative to the myosin tail -> release of ADP
121
What regulates the availability of Myosin-binding sites on actin?
Tropomyosin and troponin
122
____ causes conformation changes to tropomyosin-troponin complex exposing myosin binding sites
Ca2+
123
The ______ is stabilized by H bonds between nearby residues
Alpha helix
124
The ______ stabilized by H bonds between adjacent segments that may not be nearby
Beta sheet
125
Irregular arrangement of the polypeptide chain is called the ________
Random coil
126
What amino acids are examples of strong helix formers?
Alanine and Leucine
127
What amino acids act as Helix breakers?
Proline and Glycine
128
What affects formation of helix and its stability?
Attractive or repulsive interactions between side chains 3-4 amino acids apart
129
What 5 amino acids are common in beta sheets?
```
Valine
Isoleucine
Tyrosine
Cysteine
Tryptophan
```
130
In _____ beta sheets the H-bonded strands run in the same direction
Parallel
131
In ______ beta sheets the H bonded strands run in opposite directions
Antiparallel
132
_______ beta sheets results in bent H bonds
Parallel
133
________ beta sheets result in linear H bonds
Antiparallel
134
________ beta sheets are stronger than ______ beta sheets
Antiparallel; parallel
135
What 3 amino acids are common in beta turns?
Proline
Glycine
Asparagine
136
What amino acid is common in type 1 beta turns?
Proline
137
What amino acid is common in type 2 beta turn?
Glycine
138
What does the tertiary structure refer to?
The overall spatial arrangement fo atoms in a protein
139
What are the two major classes of tertiary structure?
Fibrous and globular ( water or lipid soluble)
140
______ proteins always have combination of secondary structures and turns are always present
______ protein mostly one type of secondary structure
Globular
Fibrous
141
_______ proteins are practically insoluble
_____ proteins are fully soluble or membrane bound
Fibrous
Globular
142
The main function of ______ proteins are mostly dynamic roles
The main function of ____ proteins are mostly structural roles
Globular
Fibrous
143
______ proteins are located mostly intracellularly while ______ proteins are located mostly extracellualrly
Globular
| Fibrous
144
What are examples of globular proteins?
Hemoglobin
Myoglobin
Enzymes
145
What are examples of fibrous proteins?
Collagen
Keratin
Elastin
146
_______ proteins are mostly primary and secondary structures while ______ proteins all have tertiary structures (simple) and many complex have quaternary structure
Fibrous; Globular
147
_____ proteins provide support for cells and tissues
Fibrous
148
______ is an important constituent of CT
Collagen
149
What is each collagen chain made of?
Long glycine and proline rich left handed helix
150
Three collagen chains intertwine into what?
A right handed superhelical triple helix
151
Many ________ assemble into a collagen fibril
Triple helicies
152
Type 1 collagen is present in what 5 tissues?
```
Skin
Bone
Tendon
Blood vessels
Cornea
```
153
Type 2 collagen is present in what 3 tissues?
Cartilage
Intervertebral disk
Vitreous body
154
Type 3 collagen is present in what 3 tissues?
Blood vessels skin and muscle
155
What types of collagen are fibril forming?
Type 1, 2 and 3
156
What types of collagen are network forming?
Type 4 and type 8
157
What types of collagen are fibril associated?
Type 9 and type 12
158
In the synthesis and processing of collagen what occurs inside the cells?
- Synthesis of pro-alpha-chains on ribosome ER to facilitate secretion
- Hydroxylation of selected Pro and Lys residues catalyzed by Pro and Lys hydroxylases
- Glycosylation of selected OH-Lys residues via an enzyme catalyzed process
- Spontaneous process of triple helix formation of Pro-collagen molecule
- Secretion of procollagen molecule
159
In synthesis and processing of collagen, what processes occur outside cells?
- Cleavage of extension peptides (may take place before secretion)
- Assembly into micro fibril
- Crosslink formation
- Assembly into mature collagen fibril
- Aggregation of collage fibrils to form a collagen fiber
160
Cleavage of extension peptides occurs ________ cells and is catalyzed by what?
Outside cells
Catalyzed by procollagen peptidases
161
What are the spontaneous processes that occur outside the cell in the synthesis and processing of collagen?
Assembly into micro fibril
Assembly into mature collagen fibril
Aggregation of collagen fibrils to form a collagen fiber
162
What causes cross-link formation in synthesis and processing of collagen?
Lysyl oxidase
163
What collagen genetic disease is associated with type 1 collagen?
Osteogenesis imperfecta
| -weak bones that fracture easily
164
What collagen genetic disease is associated with type 2?
Chondriodysplasias
| -abnormal cartilage, bone and joint deformities
165
What collagen genetic diseases are associated with type III and type V
Ehlers- Danlos syndrome
Fragile skin and blood vessels (type III aorta rupture) and hyper- mobile joints (type V)
166
What are motifs (folds)?
Specific arrangement of several secondary structure elements
167
___________ structure is formed by the assembly of individual polypeptides into a larger functional cluster
Quaternary
168
What are intrinsically disorder proteins composed of (amino acids)?
Composed of amino acids whose higher concentration forces less defined structure
Lys, Arg, Glu, and Pro
169
_________ _______ proteins facilitate interaction with numerous different partner proteins
Intrinsically disordered proteins
170
A proteins function depends on what?
It’s 3D structure
171
Loss of structural integrity with accompanying loss of activity is called __________
Denaturation
172
What denatures proteins?
```
Heat or cold
pH extremes
Detergents
Reducing agents: DTT and Mercaptoethanol
Chaotropic agents: urea
```
173
What reduces disulfide bonds?
Beta-Mercaptoethanol
174
Adding a chaotropic agent will _____ the protein but when the chaotropic agent is removed it causes the ______ of the protein and that protein is now catalytically active
Denature
| Renature
175
What are 4 examples of protein misfolding and neurodiseases?
Alzheimer’s disease
Parkinson’s disease
Huntington’s disease
Prion disease
176
Alzheimer’s, Parkinson’s, Huntington and creutzfeldt- Jakob diseases result in deposition of protein aggregates called ______
Amyloid fibrils or plaques
177
Alzheimer’s, Parkinson’s, Huntington’s and creutzfeldt Jakob’s disease are called ______
Amyloidoses
178
What is a common feature of amyloidoses?
Normally soluble proteins are converted into insoluble fibrils rich in beta sheets
179
What is the major proteopathy in Parkinson’s disease?
Alpha-synuclein
180
Alpha-synuclein can form insoluble aggregates or ______________ that are a major part of Parkinson’s disease
Lewy bodies
181
Where is the site of synthesis of pepsinogen?
Stomach
182
What is the site of synthesis for chymotrypsinogen, trypsinogen, procarboxypeptidase and proeleastase?
Pancreas
183
What activates trypsinogen into trypsin?
Enteropeptidase
184
What activates chymotrypsinogen, proelastase and procarboxypeptidase?
Trypsin
185
What activates pepsinogen, what is its source, and what is its target?
[H+]/ pepsin activates
Source is the stomach
Target is Phe
186
What activates trypsinogen, what is its source and what is its target?
Enteropeptidase and trypsin activates it
Source is pancreas
Target is lys and arginine residues
187
What activates chymotrypsin, what is its source and what’s its target?
Trypsin and chymotrypsin activates it
Source is the pancreas
Targets aromatic and bulky amino acids
188
Different carriers transport the families of amino acids based on what?
The nature of the R groups
189
In protein digestion and absorption, free amino acids use secondary active transport using what type of gradient?
Sodium concentraiton gradient
190
What are enzymes?
Catalysts that increase reaction rates without being used up
191
What are examples of oxidoreductases?
Dehydrogenases
Reductases
Oxidase
192
What are examples of transferase?
Kinase and transaminases
193
What are examples of hydrolases?
Lipase and proteases
194
What are examples of lyases?
Anhydrases
Dehydratases
Hydratases
195
What are examples of isomerases?
Isomerase
Mutase
Epimerases
196
What are examples of ligases?
Carboxylases and synthetase
197
_______ are required by inactive app-enzymes to convert them into active holo-enzymes
Cofactors
198
What activated carriers carry electrons?
NADH, NADPH
FADH2
FMNH2
199
What activated carrier carries phosphoryl group?
ATP
200
What activated carrier carries an aldehyde?
Thiamine pyrophosphate
201
What activated carrier carries CO2?
Biotin
202
What activated carrier carries one carbon units?
THF (tetrahydrofolate)
203
What activated carrier carries glucose?
UDP- glucose (uridine diphophate glucose)
204
Enzymes alter only the ________ and not the _________
Reaction rate
Not the equilibrium
205
Enzyme ________ ______. Are complimentary to the transition state of the reaction
Active sites
206
Enzymes bind to __________ better than substrates
Transition states
207
The ________ of enzymes is a 3D cleft or crevice that takes up a small part of the total volume of an enzyme
Active site
208
How do substrates bind to the enzyme?
By multiple weak interactions depending on the precisely defined arrangement of atoms in an active site
209
Define Vmax
Maximal velocity when the enzyme is saturated with substrate
210
Nonlinear michaelis-menten plot should be used to calculate what?
Km and Vmax
211
Linearized double-reciprocal plot is good for what?
Analysis of two-substrate data or inhibition
212
What processes take place in the mitochondria?
TCA cycle
FA oxidation
Oxidation of pyruvate
213
What cellular processes occur in the cytosol?
Glycolysis
Pentose phosphate pathway
FA synthesis
214
What cellular processes occur in the nucleus?
DNA and RNA synthesis
215
What cellular processes occur in the lysosome?
Degradation of complex macromolecules
216
What are the factors that affect reaction velocity?
Substrate concentration
Temperature
pH
217
Large Km = ______ affinity of enzyme for substrate
| Small Km = ______ affinity of enzyme for substrate
High Km= low affinity
Low Km= high affinity
218
At low concentration of substrate, the velocity of the reaction is what?
Proportional to the substrate concentration
| First order
219
What high concentration of substrate, the velocity of the reaction is what?
constant and independent of substrate concentration
| Zero order
220
T/F: allosteric enzymes do obey Michaelis-Menten kinetics
False; they do not obey Michaelis-Menten kinetics
221
Kinetics of allosteric enzymes display _______
Cooperativity
222
What is cooperativity?
Binding of substrate to one active site faciliatates the binding of the substrate to the other active sites
223
In competitive inhibition, what does the inhibitor bind to and how does it effect the Km and Vmax
Inhibitor binds to Enzyme only
Raises Km
Vmax unchanged
224
In uncompetitive inhibition, what does the inhibitor bind to and what is its effect on Km and Vmax?
Inhibitor binds to enzyme substrate ONLY
Lowers both Km and Vmax
Ratio Km/Vmax remains unchanged
225
In noncompetitive inhibition, what does the inhibitor bind to? And what its its effect on Km and Vmax?
Inhibitor binds to enzyme OR enzyme substrate complex
Lowers Vmax
Km remains unchanged
226
Describe feedback inhibition
The products of one pathway will inhibit further production of that product
227
What are examples of regulation of enzyme activity?
Feedback inhibition
| Covalent modification
228
What are examples of covalent modification?
The addition and removal of phosphate groups
229
Zymogen activation and the blood coagulation cascade use what?
Irreversible covalent modification
230
What are the two most common types of cofactors?
Inorganic ions (metal) and coenzymes
231
Apoenzyme = ______
Holoenzyme= _______
Apoenzyme + cofactor -> _________
Inactive
Active
Holoenzyme
232
What is the cofactor for pyruvate dehydrogenase?
Thiamine pyrophosphate
233
What is the cofactor for pyruvate carboxylase?
Biotin
234
What is the cofactor for Lactate dehydrogenase?
Nicotinamide adenine nucleotide
235
What is the cofactor for methylamlonyl mutase?
5’ deoxyadenosyl cobalamin
236
What is the cofactor for thymidylate synthase?
Tetrahydrofolate (THF)
237
What is the cofactor for carbonic anhydrase?
Zn2+
238
What is the cofactor for hexokinase?
Mg2+
239
What is the cofactor for glutathione peroxidase?
Se
240
What is the cofactor for superoxide dismutase?
Mn
