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Biochemistry 1 > Exam 2 > Flashcards

Exam 2 Flashcards

1
Q

Most abundant biomolecule in the body

A

Proteins

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2
Q

Proteins _______ every process in the cell

A

MEDIATE every process

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3
Q

Building blocks of proteins

A

amino acids

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4
Q

There are ___ total amino acids.
_________ was the first discovered in 1806.
_________ was the last discovered in 1908

A

20 total
Asparagine (1806)
Threonine (1938)

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5
Q

All amino acids are anchored to an __ carbon

A

(alpha) carbon

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6
Q

All amino acids have chiral center except…

A

Glycine

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7
Q

Almost all carboxyl and amino groups are bound in _______ bond.

A

Peptide

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8
Q

L - Amino Acid (acronym + direction)

A

CORN clockwise

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9
Q

D - Amino Acid (acronym + direction)

A

CORN counter clockwise

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10
Q

Amino acid that contains a hydrocarbon is __________.

A

Aliphatic

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11
Q

_______ (nonpolar) replaces glutamine (polar) in hemoglobin.

causes it to fold incorrectly

A

Valine (replaces glutamine)

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12
Q

Valine replacing glutamine causes hemoglobin to fold incorrectly. This is know as ______ _____ ______

A

Sickle Cell Anemia

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13
Q

Genetic deficiency of enzymes required to metabolize branched chain amino acids.

A

Maple Syrup Urine Disease

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14
Q

Methionine and Proline are ________ _______ R groups

A

Nonpolar Aliphatic

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15
Q

Leucine, Isoleucine and Valine are nonpolar aliphatic R groups with….

A

Branched Chain Amino Acids

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16
Q

Gluten = _______ + ________

A

Gliadin + Glutenin

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17
Q

_______ is the alcohol-soluble portion in wheat.

A

Gliadin

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18
Q

Genetic disorder that lacks enzyme necessary to metabolize phenylalanine

A

Phenylketonuria (PKU)

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19
Q

Phenylketonuria:
Causes…
__/_______ babies born with
Treatment:

A

Phenylketonuria:
Causes BRAIN DAMAGE.
1/10,000 babies born with.
Treatment: Avoid PHENYLALANINE

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20
Q

Phenylalanine is found in… (2)

A

Nutrasweet

Anything with protein

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21
Q

Most common disorder

A

Cystic Fibrosis

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22
Q

Cystic Fibrosis:
_______ disorder affecting __/______ humans.
Missing __ __________ in protein that regulates transport of chloride ions across cell membranes.

A

Cystic Fibrosis:
GENETIC disorder affecting 1/2,000 humans.
Missing 1 PHENYLALANINE in protein that regulates transport of chloride ions across cell membranes.

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23
Q

Cystine =

A

Disulfide Bridge

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24
Q

_______ and _______ are 2 of many proteins stabalized by disulfide bridges.

A

Albumin

Insulin

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25
Precursor for nitric oxide.
Arginine
26
Precursor for histmaine
Histidine
27
Amyloids: - Normal cellular proteins that ________ and _______ _________. - _______ is key for holding it together through __________ and __________ interactions.
Amyloids: - Normal cellular proteins that UNRAVEL and STICK TOGETHER. - LYSINE is key for holding it together through HYDROPHOBIC and ELECTROSTATIC interactions.
28
Tangles: (2)
Microtubules become phosphorylated and behave unnaturally. | Accumulation can cause them to ruptore/
29
Alzheimer's Disease Proteins: (2)
Amyloids | Tangles
30
New, potential treatment for alzheimers:
CLR01 binds to lysine and arginine
31
____ of all glutamate is used by the cells lining the _____ _______. So, very little enters the __________
90% of all glutamate is used by cells lining the SMALL INTESTINE. So, very little enters the BLOODSTREAM
32
The brain makes its own glutamate, which is turned into _____ (_____ _______)
GABA (quiet neurons)
33
MSG
Monosodium Glutamate
34
The major amino acid in plants
Glutamate
35
Precursor to dopamine
Tyrosine
36
9 essential amino acids
``` (PVT MT HILL) Phenylalanine Valine Tryptophan Methionine Threonine Histidine Isoleucine Lysine Leucine ```
37
Nonessential Glucogenic only (10)
``` (AAAA C GGG PS) Alanine, Arginine, Asparagine, Aspartate, Cysteine, Glutamate, Glutamine, Glycine, Proline, Serine ```
38
Essential Glucogenic only (4)
Histidine Methionine Threonine Valine
39
Nonessential Glucogenic and Ketogenic
Tyrosine
40
Essential Glucogenic and Ketogenic (3)
Isoleucine Phenylalanine Tryptophan
41
Essential Ketogenic only (2)
("Lindsey Lohan = Fat Only") Leucine Lysine
42
2 uncommon amino acids found in collagen
Hydroxyproline | Hydroxylysine
43
Methyllysine
Part of myosin
44
Desmosine
Part of elastin
45
Carboxyglutamate (2)
2 carboxylic acids total | Found in proteins that stimulate clotting and bone synthesis
46
Selenocysteine
Special amino acid derivative that uses selenium instead of sulfur
47
When pH is high, amino acids can...
Donate H+
48
When it comes to donating and accepting protons, the proton donor is always the ________ group and the proton acceptor is always the ________ group
Proton Donor - AMINO group | Proton Acceptor - Carboxyl group
49
When pH is _____, amino acids can accept H+
Low
50
Compounds that can act as an acid and base
Amphoteric
51
If pH is below pK... | If pH is above pK...
below pK = H is still attached | above pK = H is lost
52
pK1 is the removal of H from the ______ group. pK2 is the removal of H from the ______ group. pKr is the removal of H from the ______ group.
``` pK1 = removal from CARBOXYL group pK2 = removal from AMINO group pKr = removal from R group ```
53
If pH is below both pK1 and pK2... (2)
Both pK1 and pK2 are PROTONATED (fully protonated) | Both H still attached
54
________: Amino group and carboxyl group cancel each other out - no charge.
Zwitterion
55
When pH is above pK1 and pKr, but below pK2, net charge = ___
net charge = -1 | H on pK1 and pKr is lost... H still attached to amino group
56
______ ________: pH is above pK1, pKr and pK2. | Net Charge = ____
Fully Deprotonated | Net Charge = -2 (carboxyl and R group become negatively charged and amino group becomes neutral)
57
The point where an AA or protein is neutral (zwitterion)
Isoelectric Point
58
Chains of amino acids
Peptides
59
Peptides: Contains peptide bond formed by ________. Many amino acids is called a _________.
Dehydration - removal of 1 H2O for each peptide bond | Polypeptide
60
Proteins: Chains of amino acids... Contains ________ bonds
Proteins: chains of amino acids WITH MOLECULAR WEIGHT >10,000 contains PEPTIDE bonds
61
3D structure of a protein is determined by its...
Amino Acid Sequence
62
The most important stabilizing force for protein structures are...
Noncovalent Interactions
63
Protein structures are (static/dynamic)
DYNAMIC - NOT static
64
________: Spatial arrangement of atoms in a protein.
Conformation
65
_______: Proteins in their functional, folded conformation. - -
Native - most stable - has lowest Gibbs free energy
66
_______: Proteins ability to maintain the native conformation. Held together by...
Stability | Held together by DISULFIDE bonds and WEAK (NONCOVALENT) INTERACTIONS.
67
Simple Rules of Protein Structure: Hydrophobic amino acids are... _______ and __________ interactions are maximized within the protein
Hydrophobic amino acids are BURIED in the middle of the structure, away from water. H BONDS and ELECTROSTATIC interactions are maximized within the protein
68
Levels of Protein Structure: | Primary: (2)
Sequence of amino acids | Includes covalent bonding (peptide bonds)
69
Peptide bonds are formed via...
Condensation/Dehydration reactions
70
________ = 2 AA Polypeptide = ___ - ___ AA >_____ AA is a protien
``` DIPEPTIDE = 2 AA Polypeptide = 10-100 AA Protein = >100 AA ```
71
Synthesis of all macronutrients are _________ reactions
Dehydration
72
Polypeptide backbone is rich in ________ and ______ groups which are great at _________ ________.
Polypeptide backbone is rich in CARBONYLS and AMINO groups which are great at HYDROGEN BONDING
73
Most polypeptides are ___-_____ AA residues in length
50-2,000 AA
74
_______ - Largest known protein. | _______ AA residues
Titin | 27,000 AA residues
75
Protein Secondary Structure Arrangements: (3) | All held together by...
Alpha Helix Beta Sheets Beta Turns held together by H-BONDS
76
The overall 3D structure of the protein
Tertiary Structure
77
Tertiary structure is held together by: (2)
Covalent Bonds - Disulfide Bridges | Noncovalent Bonds - Electrostatic, H-bonding, hydrophobic
78
_______: 2 or more separate polypeptides in a protein | Quaternary Structure:
Subunits | Quaternary Structure: Subunits fold together to form a protein
79
Quaternary structures are held together by...
Noncovalent interactions - electrostatic, H-bonding, hydrophobic
80
Types of proteins: (2)
Fibrous | Globular
81
Fibrous Proteins: Contain... Function as...
Contain single secondary structure | Function as providers of support, shape and external protection
82
Globular Proteins: - Contain... - Function as... -
- Contain several secondary structures - Function as enzymes, regulatory proteins, transport molecules, immunoglobulins - Water-Soluble
83
Fibrous Proteins: Contain mostly ________ structures. Further stabalized by ________ _______. Most common: (2)
Fibrous Proteins: Contains mostly SECONDARY structures. Further stabilized by DISULFIDE BRIDGES. Most common: Keratin and Collagen
84
Keratin: Found in... Contains...
Found in HAIR and NAILS | Contains 2 right-handed alpha helices intertwined to form a superhelix called a COILED COIL
85
Collagen: Provides strength in... Contains a unique ________ structure - ... ____ different types in mammals.
Provides strength in BONE, TENDONS, CARTILAGE (connective tissue). Contains a unique SECONDARY structure - COILED COIL, but 3 POLYPEPTIDE CHAINS wound together. 30 different types on mammals
86
``` Scurvy: Due to... Which is required for... Deficiency leads to... 2 symptoms - ```
Scurvy: Due to lack of VITAMIN C Which is required for HYDROXYLATION of PROLINE and LYSINE in COLLAGEN SYNTHESIS. Deficiency leads to DEGENERATION of CONNECTIVE TISSUE. Symptoms: Corkscrew Hair, Bleeding Gums
87
Collagen and Vitamin C: Posttranslational Modification = Proline ------????-----> Hydroxyproline More Hydroxyl Groups =
Collagen and Vitamin C: Posttranslational Modification = Functional group added after protein is synthesized. Proline ------Proline Hydroxylase/ Requires Vitamin C (coenzyme) and Iron (cofactor) -----> Hydroxyproline More Hydroxyl Groups = MORE H BONDING
88
Lysyl Oxidase: (3)
Copper-Dependent Enzyme Deaminates Lysine, forming reactive aldehyde Aldehyde condenses with lysine or hydroxylysine on neighboring collagen
89
Collagen is degraded by _______ ____________
Matrix Metalloproteinases (MMPs)
90
MMPs = _______ ___________ - Main class of ________ - 'Metallo' = - Required for...
Matrix Metalloproteinases - Main class of PROTEASES - 'Metallo' = Requires Metals (Ca and Zn - Cofactors) - Required for TISSUE REMODELING
91
Globular Proteins: Nonpolar AA... Polar AA...
Nonpolar AA found in the interior, held together by hydrophobic interactions. Polar AA located in exterior.
92
Globular Proteins: Folding Patterns: (2) Protein Families: (2)
Globular Proteins: Folding Patterns: Motif - Folding of secondary structure/Not inherently stable Domain - Part of polypeptide chain that is independently stable Protein Families: Similar primary structures are clustered into families. Strong evolutionary relationship.
93
Folded proteins are in their _______ _________. | Some proteins require assisted folding thorough use of ________.
Native Conformation | Chaperones
94
Two types of protein misfolding
Degraded | Accumulated
95
Degrade protein misfolding: (2)
25% of all proteins fold incorrectly | Cystic Fibrosis
96
Accumulated protein misfolding: (2)
PKU | Amyloids in Alzheimer's
97
Like water = | Doesn't like water =
Like water = POLAR | Doesn't like water = NONPOLAR
98
Protein Unfolding Methods: (3)
Heat Strong acids/bases Mechanical
99
Two types of unstructured proteins
Intrinsically Unstructured Proteins | Metamorphic Proteins
100
___% of proteins have at least 1 unstructured region.
50%
101
Metamorphic Proteins:
Proteins that are able to form multiple structures that have different functions.
102
______ ______ AA are metabolized in muscle
Branched Chain
103
With maple syrup urine disease, one is unable to metabolize _______, ________ and ________ - _______ ______ AA
Valine, Leucine, Isoleucine - Branched Chain AA
104
Triple helix is always _______
Collagen
105
Molecule reversibly bound by a protein
Ligand
106
Ligand binds to...
Binding site
107
Ka = | Kd =
Association Constant - A measure of the affinity for the ligand to bind a protein Dissociation Constant - A measure of the release of the ligand
108
The smaller the Kd...
the TIGHTER the protein will bind the ligand
109
Examples of Hemeproteins: (4)
Myoblobin - oxygen carrier in muscles Hemeglobin - oxygen carrier in blood Neuroglobin - oxygen and nitric oxide carrier in neurons Cytoglobin - oxygen carrier in many tissues
110
Neuroglobin protects... | Cytoglobin protects...
Neuroglobin protects BRAIN from HYPOXIC conditions | Cytoglobin protects TISSUES from OXIDATIVE STRESS
111
Myoglobin: Number of polypeptides = ___% a-helices ___ different helices, terminated by _______ or _______
Polypeptides = 1 80% a helices 8 different helices, terminated by PROLINE or B-BENDS
112
Hemoglobin: Found exclusively in _____ Blood from lungs to peripheral tissue is ___% saturated. Blood from tissues to heart is ___% saturated. Number of polypeptides =
Found exclusively in RBCs Blood from lungs to peripheral tissue is 96% saturated Blood from tissues to heart is 64% saturated Number of polypeptides = 4
113
Oxyhemoglobin: (3) Deoxyhemoglobin: (3)
``` Oxyhemoglobin: Relaxed Less electrostatic interactions (ion pairs) High affinity for binding oxygen Deoxyhemoglobin: Tense More electrostatic Interactions (ion pairs) Low affinity for binding oxygen ```
114
Saturation of oxygen-binding sites varies based on...
Pressure of Oxygen (pO2)
115
Cooperative Binding:
(Hemoglobin) | Binding oxygen at one heme increases affinity for bonding oxygen at other heme sites
116
Allosteric means... Allosteric proteins have several possible structural conformations induced by binding of a type of ligand called a ________
"Other Shape" | Modulator
117
Homotropin Interactions = | Heterotropic Interactions =
``` Homotropic = Ligand and Modulator are IDENTICAL Heterotropic = Ligand and Modulator are DIFFERENT Compounds ```
118
Oxygen is both a _______ and an activating _________ modulator
Oxygen is both a LIGAND and an activating HOMOTROPIC Modulator
119
Hemoglobin has other inhibiting ________ modulators (non-oxygen): (4)
``` HETEROTROPIC Modulators: Carbon Monoxide Carbon Dioxide Hydrogen Ions 2,3-bisphosphoglycerate ```
120
2,3-bisphosphoglycerate: (3)
Decreases affinity for oxygen by stabilizing T structure Facilitates oxygen release in peripheral tissues Important for physiologic adaptation to less oxygen at high altitude
121
Binding CO (carbon monoxide): (2)
250 times higher affinity for CO and oxygen | Prevents oxygen from being released
122
Carbon Monoxide: ___% of Hb is bound to CO in healthy individuals. __-__% bound in smokers ___% bound by CO induces headache ___-___% bound causes severe headache, nausea, dizziness ___% bound results in coma and death
123
RBCs have a lifespan of...
120 days
124
Jaundice: Caused by large concentrations of _______ in _________ ______. Causes: (3)
Jaundice: Caused by large concentrations of BILIRUBIN in EXTRACELLULAR FLUID. Causes: Excessive destruction of RBC (Hemolytic Jaundice) Obstruction of Bile Duct (Obstructive Jaundice) Liver Damage (Obstructive Jaundice)
125
Hemolytic Jaundice:
High levels of free (UNCONJUGATED) bilirubin and urobilinogen in blood
126
Obstructive Jaundice: (3)
High levels of CONJUGATED bilirubin in blood No urobilinogen in urine since bile is not able to reach gut for urobilinogen synthesis Urine is foamy and VERY yellow
127
In heme, iron has the highest affinity for ____.
CO
128
Immune responses to protein are... (2)
Very Specific | Extremely Sensitive
129
Two subunits of the immune system and what they respond to (2 each)
Humoral - Bacterial Infections and Extracellular Viruses | Cellular - Cellular Viruses and Parasites
130
Proteins and Ligands in the Immune System: - Antibodies... - White Blood Cells (called _______) include: (2) - Antigen =
Antibodies (AKA Immunogloblins) aer soluble proteins White Blood Cells (called Leukocytes) include: Macrophages and Lymphocytes Antigen = Compound able to produce an immune response
131
Macrophages: (1) Lymphocytes: (2)
Macrophages: Ingest foreign particles by phagocytosis Lymphocytes: T cells - Cytotoxic T cells recognize infections and T Helper cells make signaling proteins called Cytokines B cells produce Immunoglobulins
132
Allergenic Proteins: (2) | Examples: (4)
``` Allergenic Proteins: Small, water soluble glycoproteins Difficult to denature Examples: Casein in Milk Proline-Region in gliadin (GLUTEN) Vicillin in Peanuts Ovomucoid in Egg ```
133
``` Classes of Immunoglobulins: IgG = IgA = IgE = IgM = ```
``` IgG = Most Common IgA = Found in secretions IgE = Main antibody produced in response to food allergens IgM = First antibody produced during immune response ```
134
Movement of organisms, cells, organelles, etc. is from a special class of proteins called...
Molecular Motors
135
______ and ______ make up 80% of muscle mass
Actin (thin filament) and Myosin (thick filament)
136
Two proteins that regulate interactions between actin and myosin
Tropomyosin - Binds actin and blocks myosin | Troponin - Calcium-binding protein
137
All important pathways have _______ _______ that control them
Regulatory Proteins
138
Two types of protein
Exogenous (dietary) - from animals and plants | Endogenous - from digestive enzymes and sloughed cells
139
Proteins are digested by ________
Proteases
140
Protein digestion in the stomach: (2)
PEPSINOGEN secreted by CHIEF CELLS | HCl release from PARIETAL CELLS in response to GASTRIN
141
Pepsinogen is activated by ______
HCl
142
HCl denatured which structures of proteins. | HCl converts...
Secondary Tertiary Quaternary Converts Pepsinogen (inactive) to Pepsin (active)
143
Pepsinogen/pepsin: Active at pH of ___. Inactive at pH of ___.
``` Active = pH of 2 Inactive = pH of >4.5 ```
144
Pepsinogen has ____ amino acids removed to activate and become pepsin.
46
145
Protein digestion in SI: (2)
Chyme released into SI stimulates release of SECRETIN and CCK. SECRETIN and CCK stimulate release of BICARBONATE, WATER, ELECTROLYTES and ZYMOGENS from PANCREAS.
146
________ neutralizes stomach acid. | Zymogens are _________ enzymes.
BICARBONATE neutralizes stomach acid | Zymogens are INACTIVE enzymes
147
Enzyme secreted from STOMACH. Active at secretion? End product(s)?
Pepesinogen No, activated by HCl Peptides
148
Enzymes secreted from PANCREAS: (4) Active as secretion? End product(s)?
Trypsinogen --> No, activated by Enteropeptidase --> Smaller Peptides/Amino Acids Chymotrypsinogen --> No, activated by Trypsin --> Smaller Peptides/Amino Acids Procarboxypeptidase A --> No, activated by Trypsin --> Free Amino Acids Procarboxypeptidase B --> No, activated by Trypsin --> Free Amino Acids
149
Enzymes secreted from BRUSH BORDER: (2) Active as secretion? End product(s)?
Aminopeptidase --> Yes --> Free Amino Acids | Dipeptidase --> Yes --> Free Amino Acids
150
Pancreatic and Brush Border enzymes digest proteins to free... (3)
AA Dipeptides Tripeptides
151
Most digestive products (3) | All are absorbed via ________ ________, requiring _______, _________, ______ _______ and _____
AA Dipeptides Tripeptides Absorbed via SECONDARY TRANSPORT, requiring SODIUM, POTASSIUM, CARRIER PROTEIN and ATP.
152
Peptide absorption accounts for ___% of protein absorption. | ________ absorption occurs faster than ______ absorption.
60% | Peptide absorption occurs faster than Free AA absorption
153
Once out of the enterocyte, AA reach the liver via the...
Portal Vein
154
New proteins made in liver: (3)
Enzymes Plasma Proteins Acute Phase Proteins
155
Branched Chain Amino Acids: (6) | Associated with...
``` LIV GAA Leucine Isoleucine Valine Glutamate Asparagine Asparate Associated with MUSCLES ```
156
Albumin: (3)
Most abundant plasma protein Maintains osmotic pressure Transports Nutrients
157
Globulins: (3)
Enzymes Important for Immunity Transporters
158
Fibrinogen: (1)
Important for clotting
159
Which hormone stimulates bicarbonate secretion from the pancreas into the SI?
Secretin
160
What is able to cross the basolateral membrane of enterocytes?
Free Amino Acids ONLY
161
Human genome protein-coding genes are ___% enzymes
16%
162
Biological Catalysts: | _______ Proteins: (3)
GLOBULAR Proteins: Speed up reactions with being consumed Do not shift equilibrium, just reach it faster Very specific
163
Cofactor: (definition) - (4 examples) - (category)
Cofactor: INorganic components need to work. - Fe, Mg, Zn, Se - Minerals
164
Coenzyme: (definition) - Often used to... - (7 examples) - (category)
Coenzyme: Organic component needed to work - Often used to TRANSFER CHEMICAL GROUPS - Vit. B6, Vit. B12, Thiamin, Folate, Riboflavin, Biotin, Niacin - Vitamins
165
``` Cofactor : Enzyme(s) Copper: Iron: Potassium: Magnesium: Zinc: ```
Copper: Cytochrome Oxidase Iron: Cytochrome Oxidase, Catalase, Peroxidase Potassium: Pyruvate Kinase Magnesium: Hexokinase, Glucose-6-Phosphate, Pyruvate Kinase Zinc: Alcohol Dehydrogenase, Carboxypeptidases A and B
166
``` Coenzyme : Chemical Group Transferred Biotin: Pantothenic Acid: B12 Riboflavin and Niacin: Folate: ```
``` Biotin: Carbon Dioxide Pantothenic Acid: Acyl Groups (fatty acids) B12: H atoms Riboflavin and Niacin: Electrons Folate: Methyl Groups ```
167
________ - protein part of enzyme only - Missing _________/________ ________ - Complete (active) enzyme - _______ + ________/_______
APOENZYME - protein part of enzyme only - missing COFACTOR/COENZYME HOLOENZYME - complete (active) enzyme - PROTEIN + COFACTOR/COENZYME
168
_______ - Enzyme precursor (inactive) | example
Zymogen | Trypsinogen --> Enterokinase --> Trypsin
169
6 Classes of enzymes
``` Oxidoreductase Transferase Isomerase Hydrolase Lyase Ligase ```
170
Oxidoreductase: (2)
``` Addition or removal of H Requires coenzyme (NAD and FAD) ```
171
Transferase:
Transfer a functional group from one molecule to another
172
Isomerase:
Rearrange functional group on one molecule
173
Hydrolase: (2)
Causes HYDROLYSIS reaction | Water breaks bond
174
Lyase:
Cleaves C-C, C-S or C-N bonds
175
Ligase: (2)
JOINS bond between C and another element (O, S, N) | Generally need energy from ATP
176
``` Enzymes: Reaction rate (speed) is dependant on ________ ________. How does it impact reaction rate? ```
Activation Energy Higher AE = SLOWER reaction Lower AE = FASTER reaction
177
How do catalysts work?
Catalysts speed up reactions by lowering the activation energy
178
Enzymes contain an _____ _____ which reacts with specific _______
Active Site | Substrate
179
Active Site: (2)
Binding Site: Holds substrate in proper place - weak, non-covalent interactions between AA and substrate Catalytic Site: Where reaction actually occurs
180
Vo = Vmax = Km =
``` Vo = Reaction Velocity - number of reactions catalyzed by enzyme per second Vmax = Maximum Velocity - Enzyme is completely saturated with substrate Km = Michaelis Constant - Affinity for binding (1/2 Vmax). SMALLER THE BETTER ```
181
Smaller Km =
High affinity to bind [S] (less [S] needed to reach 1/2 Vmax)
182
Irreversible Inhibitor
Covalent Bonding
183
``` Reversible Inhibitor (1) - (4 sub-points) ```
Non-Covalent Interactions - Can dissociate - Competitive - Uncompetitive - Noncompetitive
184
With competitive inhibitor... | in relation to Vo, Km, Vmax
Changes Km | Does NOT change Vmax
185
With uncompetitive inhibitor... | in relation to Vo, Km, Vmax
Both Km and Vmax change
186
With noncompetitive inhibitor... | (in relation to Vo, Km, Vmax
Changes Vmax | Does NOT change Km
187
___% of the most commonly prescribed drugs target and inhibit enzymes
50%
188
Antibiotics inhibit enzymes that make...
Proteins for their cell wall
189
Enzymes in a pathway that are easier to control.
Regulatory Enzymes
190
Common covalent modifying groups: (4)
Phosphates ---> Serine, Threonine, Tyrosine Adenine ---> Tyrosine ONLY Acetyl ---> Lysine ONLY Methyl ---> Glutamate ONLY
191
Phosphorylation:
Adding or removing phosphate group to serine, threonine or tyrosine
192
Phosphorylation of glycogen _________ increases activity.
Phosphorylase
193
Phosphorylation of glycogen ________ decreases activity
Synthase
194
Cells can regulate the amount of E by...
Induction or Repression
195
Inductions occurs from...
Hormones and Diet

Biochemistry 1 (5 decks)

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