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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
Q

Precursor for nitric oxide.

A

Arginine

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26
Q

Precursor for histmaine

A

Histidine

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27
Q

Amyloids:

  • Normal cellular proteins that ________ and _______ _________.
  • _______ is key for holding it together through __________ and __________ interactions.
A

Amyloids:

  • Normal cellular proteins that UNRAVEL and STICK TOGETHER.
  • LYSINE is key for holding it together through HYDROPHOBIC and ELECTROSTATIC interactions.
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28
Q

Tangles: (2)

A

Microtubules become phosphorylated and behave unnaturally.

Accumulation can cause them to ruptore/

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29
Q

Alzheimer’s Disease Proteins: (2)

A

Amyloids

Tangles

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30
Q

New, potential treatment for alzheimers:

A

CLR01 binds to lysine and arginine

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31
Q

____ of all glutamate is used by the cells lining the _____ _______. So, very little enters the __________

A

90% of all glutamate is used by cells lining the SMALL INTESTINE. So, very little enters the BLOODSTREAM

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32
Q

The brain makes its own glutamate, which is turned into _____ (_____ _______)

A

GABA (quiet neurons)

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33
Q

MSG

A

Monosodium Glutamate

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34
Q

The major amino acid in plants

A

Glutamate

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35
Q

Precursor to dopamine

A

Tyrosine

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36
Q

9 essential amino acids

A 
(PVT MT HILL)
Phenylalanine
Valine
Tryptophan
Methionine
Threonine
Histidine
Isoleucine
Lysine
Leucine
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37
Q

Nonessential Glucogenic only (10)

A 
(AAAA C GGG PS)
Alanine, Arginine, Asparagine, Aspartate,
Cysteine,
Glutamate, Glutamine, Glycine,
Proline, Serine
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38
Q

Essential Glucogenic only (4)

A

Histidine
Methionine
Threonine
Valine

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39
Q

Nonessential Glucogenic and Ketogenic

A

Tyrosine

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40
Q

Essential Glucogenic and Ketogenic (3)

A

Isoleucine
Phenylalanine
Tryptophan

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41
Q

Essential Ketogenic only (2)

A

(“Lindsey Lohan = Fat Only”)
Leucine
Lysine

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42
Q

2 uncommon amino acids found in collagen

A

Hydroxyproline

Hydroxylysine

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43
Q

Methyllysine

A

Part of myosin

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44
Q

Desmosine

A

Part of elastin

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45
Q

Carboxyglutamate (2)

A

2 carboxylic acids total

Found in proteins that stimulate clotting and bone synthesis

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46
Q

Selenocysteine

A

Special amino acid derivative that uses selenium instead of sulfur

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47
Q

When pH is high, amino acids can…

A

Donate H+

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48
Q

When it comes to donating and accepting protons, the proton donor is always the ________ group and the proton acceptor is always the ________ group

A

Proton Donor - AMINO group

Proton Acceptor - Carboxyl group

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49
Q

When pH is _____, amino acids can accept H+

A

Low

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50
Q

Compounds that can act as an acid and base

A

Amphoteric

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51
Q

If pH is below pK…

If pH is above pK…

A

below pK = H is still attached

above pK = H is lost

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52
Q

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.

A 
pK1 = removal from CARBOXYL group
pK2 = removal from AMINO group
pKr = removal from R group
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53
Q

If pH is below both pK1 and pK2… (2)

A

Both pK1 and pK2 are PROTONATED (fully protonated)

Both H still attached

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54
Q

________: Amino group and carboxyl group cancel each other out - no charge.

A

Zwitterion

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55
Q

When pH is above pK1 and pKr, but below pK2, net charge = ___

A

net charge = -1

H on pK1 and pKr is lost… H still attached to amino group

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56
Q

______ ________: pH is above pK1, pKr and pK2.

Net Charge = ____

A

Fully Deprotonated

Net Charge = -2 (carboxyl and R group become negatively charged and amino group becomes neutral)

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57
Q

The point where an AA or protein is neutral (zwitterion)

A

Isoelectric Point

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58
Q

Chains of amino acids

A

Peptides

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59
Q

Peptides:
Contains peptide bond formed by ________.
Many amino acids is called a _________.

A

Dehydration - removal of 1 H2O for each peptide bond

Polypeptide

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60
Q

Proteins:
Chains of amino acids…
Contains ________ bonds

A

Proteins:
chains of amino acids WITH MOLECULAR WEIGHT >10,000
contains PEPTIDE bonds

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61
Q

3D structure of a protein is determined by its…

A

Amino Acid Sequence

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62
Q

The most important stabilizing force for protein structures are…

A

Noncovalent Interactions

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63
Q

Protein structures are (static/dynamic)

A

DYNAMIC - NOT static

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64
Q

________: Spatial arrangement of atoms in a protein.

A

Conformation

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65
Q

-

A

Native

  • most stable
  • has lowest Gibbs free energy
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66
Q

_______: Proteins ability to maintain the native conformation.
Held together by…

A

Stability

Held together by DISULFIDE bonds and WEAK (NONCOVALENT) INTERACTIONS.

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67
Q

Simple Rules of Protein Structure:
Hydrophobic amino acids are…
_______ and __________ interactions are maximized within the protein

A

Hydrophobic amino acids are BURIED in the middle of the structure, away from water.
H BONDS and ELECTROSTATIC interactions are maximized within the protein

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68
Q

Levels of Protein Structure:

Primary: (2)

A

Sequence of amino acids

Includes covalent bonding (peptide bonds)

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69
Q

Peptide bonds are formed via…

A

Condensation/Dehydration reactions

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70
Q

________ = 2 AA
Polypeptide = ___ - ___ AA
>_____ AA is a protien

A 
DIPEPTIDE = 2 AA
Polypeptide = 10-100 AA
Protein = >100 AA
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71
Q

Synthesis of all macronutrients are _________ reactions

A

Dehydration

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72
Q

Polypeptide backbone is rich in ________ and ______ groups which are great at _________ ________.

A

Polypeptide backbone is rich in CARBONYLS and AMINO groups which are great at HYDROGEN BONDING

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73
Q

Most polypeptides are ___-_____ AA residues in length

A

50-2,000 AA

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74
Q

_______ - Largest known protein.

_______ AA residues

A

Titin

27,000 AA residues

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75
Q

Protein Secondary Structure Arrangements: (3)

All held together by…

A

Alpha Helix
Beta Sheets
Beta Turns
held together by H-BONDS

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76
Q

The overall 3D structure of the protein

A

Tertiary Structure

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77
Q

Tertiary structure is held together by: (2)

A

Covalent Bonds - Disulfide Bridges

Noncovalent Bonds - Electrostatic, H-bonding, hydrophobic

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78
Q

_______: 2 or more separate polypeptides in a protein

Quaternary Structure:

A

Subunits

Quaternary Structure: Subunits fold together to form a protein

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79
Q

Quaternary structures are held together by…

A

Noncovalent interactions - electrostatic, H-bonding, hydrophobic

80
Q

Types of proteins: (2)

A

Fibrous

Globular

81
Q

Fibrous Proteins:
Contain…
Function as…

A

Contain single secondary structure

Function as providers of support, shape and external protection

82
Q

Globular Proteins:
- Contain…
- Function as…
-

A
  • Contain several secondary structures
  • Function as enzymes, regulatory proteins, transport molecules, immunoglobulins
  • Water-Soluble
83
Q

Fibrous Proteins:
Contain mostly ________ structures.
Further stabalized by ________ _______.
Most common: (2)

A

Fibrous Proteins:
Contains mostly SECONDARY structures.
Further stabilized by DISULFIDE BRIDGES.
Most common: Keratin and Collagen

84
Q

Keratin:
Found in…
Contains…

A

Found in HAIR and NAILS

Contains 2 right-handed alpha helices intertwined to form a superhelix called a COILED COIL

85
Q

Collagen:
Provides strength in…
Contains a unique ________ structure - …
____ different types in mammals.

A

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
Q 
Scurvy:
Due to...
Which is required for...
Deficiency leads to...
2 symptoms -
A

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
Q

Collagen and Vitamin C:
Posttranslational Modification =
Proline ——????—–> Hydroxyproline
More Hydroxyl Groups =

A

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
Q

Lysyl Oxidase: (3)

A

Copper-Dependent Enzyme
Deaminates Lysine, forming reactive aldehyde
Aldehyde condenses with lysine or hydroxylysine on neighboring collagen

89
Q

Collagen is degraded by _______ ____________

A

Matrix Metalloproteinases (MMPs)

90
Q

MMPs = _______ ___________

  • Main class of ________
  • ‘Metallo’ =
  • Required for…
A

Matrix Metalloproteinases

  • Main class of PROTEASES
  • ‘Metallo’ = Requires Metals (Ca and Zn - Cofactors)
  • Required for TISSUE REMODELING
91
Q

Globular Proteins:
Nonpolar AA…
Polar AA…

A

Nonpolar AA found in the interior, held together by hydrophobic interactions.
Polar AA located in exterior.

92
Q

Globular Proteins:
Folding Patterns: (2)
Protein Families: (2)

A

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
Q

Folded proteins are in their _______ _________.

Some proteins require assisted folding thorough use of ________.

A

Native Conformation

Chaperones

94
Q

Two types of protein misfolding

A

Degraded

Accumulated

95
Q

Degrade protein misfolding: (2)

A

25% of all proteins fold incorrectly

Cystic Fibrosis

96
Q

Accumulated protein misfolding: (2)

A

PKU

Amyloids in Alzheimer’s

97
Q

Like water =

Doesn’t like water =

A

Like water = POLAR

Doesn’t like water = NONPOLAR

98
Q

Protein Unfolding Methods: (3)

A

Heat
Strong acids/bases
Mechanical

99
Q

Two types of unstructured proteins

A

Intrinsically Unstructured Proteins

Metamorphic Proteins

100
Q

___% of proteins have at least 1 unstructured region.

A

50%

101
Q

Metamorphic Proteins:

A

Proteins that are able to form multiple structures that have different functions.

102
Q

______ ______ AA are metabolized in muscle

A

Branched Chain

103
Q

With maple syrup urine disease, one is unable to metabolize _______, ________ and ________ - _______ ______ AA

A

Valine, Leucine, Isoleucine - Branched Chain AA

104
Q

Triple helix is always _______

A

Collagen

105
Q

Molecule reversibly bound by a protein

A

Ligand

106
Q

Ligand binds to…

A

Binding site

107
Q

Ka =

Kd =

A

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
Q

The smaller the Kd…

A

the TIGHTER the protein will bind the ligand

109
Q

Examples of Hemeproteins: (4)

A

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
Q

Neuroglobin protects…

Cytoglobin protects…

A

Neuroglobin protects BRAIN from HYPOXIC conditions

Cytoglobin protects TISSUES from OXIDATIVE STRESS

111
Q

Myoglobin:
Number of polypeptides =
___% a-helices
___ different helices, terminated by _______ or _______

A

Polypeptides = 1
80% a helices
8 different helices, terminated by PROLINE or B-BENDS

112
Q

Hemoglobin:
Found exclusively in _____
Blood from lungs to peripheral tissue is ___% saturated.
Blood from tissues to heart is ___% saturated.
Number of polypeptides =

A

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
Q

Oxyhemoglobin: (3)
Deoxyhemoglobin: (3)

A 
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
Q

Saturation of oxygen-binding sites varies based on…

A

Pressure of Oxygen (pO2)

115
Q

Cooperative Binding:

A

(Hemoglobin)

Binding oxygen at one heme increases affinity for bonding oxygen at other heme sites

116
Q

Allosteric means…
Allosteric proteins have several possible structural conformations induced by binding of a type of ligand called a ________

A

“Other Shape”

Modulator

117
Q

Homotropin Interactions =

Heterotropic Interactions =

A 
Homotropic = Ligand and Modulator are IDENTICAL
Heterotropic = Ligand and Modulator are DIFFERENT Compounds
118
Q

Oxygen is both a _______ and an activating _________ modulator

A

Oxygen is both a LIGAND and an activating HOMOTROPIC Modulator

119
Q

Hemoglobin has other inhibiting ________ modulators (non-oxygen): (4)

A 
HETEROTROPIC Modulators:
Carbon Monoxide
Carbon Dioxide
Hydrogen Ions
2,3-bisphosphoglycerate
120
Q

2,3-bisphosphoglycerate: (3)

A

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
Q

Binding CO (carbon monoxide): (2)

A

250 times higher affinity for CO and oxygen

Prevents oxygen from being released

122
Q

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

A
123
Q

RBCs have a lifespan of…

A

120 days

124
Q

Jaundice:
Caused by large concentrations of _______ in _________ ______.
Causes: (3)

A

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
Q

Hemolytic Jaundice:

A

High levels of free (UNCONJUGATED) bilirubin and urobilinogen in blood

126
Q

Obstructive Jaundice: (3)

A

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
Q

In heme, iron has the highest affinity for ____.

A

CO

128
Q

Immune responses to protein are… (2)

A

Very Specific

Extremely Sensitive

129
Q

Two subunits of the immune system and what they respond to (2 each)

A

Humoral - Bacterial Infections and Extracellular Viruses

Cellular - Cellular Viruses and Parasites

130
Q

Proteins and Ligands in the Immune System:

  • Antibodies…
  • White Blood Cells (called _______) include: (2)
  • Antigen =
A

Antibodies (AKA Immunogloblins) aer soluble proteins
White Blood Cells (called Leukocytes) include: Macrophages and Lymphocytes
Antigen = Compound able to produce an immune response

131
Q

Macrophages: (1)
Lymphocytes: (2)

A

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
Q

Allergenic Proteins: (2)

Examples: (4)

A 
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
Q 
Classes of Immunoglobulins:
IgG =
IgA = 
IgE = 
IgM =
A 
IgG = Most Common
IgA = Found in secretions
IgE = Main antibody produced in response to food allergens
IgM = First antibody produced during immune response
134
Q

Movement of organisms, cells, organelles, etc. is from a special class of proteins called…

A

Molecular Motors

135
Q

______ and ______ make up 80% of muscle mass

A

Actin (thin filament) and Myosin (thick filament)

136
Q

Two proteins that regulate interactions between actin and myosin

A

Tropomyosin - Binds actin and blocks myosin

Troponin - Calcium-binding protein

137
Q

All important pathways have _______ _______ that control them

A

Regulatory Proteins

138
Q

Two types of protein

A

Exogenous (dietary) - from animals and plants

Endogenous - from digestive enzymes and sloughed cells

139
Q

Proteins are digested by ________

A

Proteases

140
Q

Protein digestion in the stomach: (2)

A

PEPSINOGEN secreted by CHIEF CELLS

HCl release from PARIETAL CELLS in response to GASTRIN

141
Q

Pepsinogen is activated by ______

A

HCl

142
Q

HCl denatured which structures of proteins.

HCl converts…

A

Secondary
Tertiary
Quaternary
Converts Pepsinogen (inactive) to Pepsin (active)

143
Q

Pepsinogen/pepsin:
Active at pH of ___.
Inactive at pH of ___.

A 
Active = pH of 2
Inactive = pH of >4.5
144
Q

Pepsinogen has ____ amino acids removed to activate and become pepsin.

A

46

145
Q

Protein digestion in SI: (2)

A

Chyme released into SI stimulates release of SECRETIN and CCK.
SECRETIN and CCK stimulate release of BICARBONATE, WATER, ELECTROLYTES and ZYMOGENS from PANCREAS.

146
Q

________ neutralizes stomach acid.

Zymogens are _________ enzymes.

A

BICARBONATE neutralizes stomach acid

Zymogens are INACTIVE enzymes

147
Q

Enzyme secreted from STOMACH.
Active at secretion?
End product(s)?

A

Pepesinogen
No, activated by HCl
Peptides

148
Q

Enzymes secreted from PANCREAS: (4)
Active as secretion?
End product(s)?

A

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
Q

Enzymes secreted from BRUSH BORDER: (2)
Active as secretion?
End product(s)?

A

Aminopeptidase –> Yes –> Free Amino Acids

Dipeptidase –> Yes –> Free Amino Acids

150
Q

Pancreatic and Brush Border enzymes digest proteins to free… (3)

A

AA
Dipeptides
Tripeptides

151
Q

Most digestive products (3)

All are absorbed via ________ ________, requiring _______, _________, ______ _______ and _____

A

AA
Dipeptides
Tripeptides
Absorbed via SECONDARY TRANSPORT, requiring SODIUM, POTASSIUM, CARRIER PROTEIN and ATP.

152
Q

Peptide absorption accounts for ___% of protein absorption.

________ absorption occurs faster than ______ absorption.

A

60%

Peptide absorption occurs faster than Free AA absorption

153
Q

Once out of the enterocyte, AA reach the liver via the…

A

Portal Vein

154
Q

New proteins made in liver: (3)

A

Enzymes
Plasma Proteins
Acute Phase Proteins

155
Q

Branched Chain Amino Acids: (6)

Associated with…

A 
LIV GAA
Leucine
Isoleucine
Valine
Glutamate
Asparagine
Asparate
Associated with MUSCLES
156
Q

Albumin: (3)

A

Most abundant plasma protein
Maintains osmotic pressure
Transports Nutrients

157
Q

Globulins: (3)

A

Enzymes
Important for Immunity
Transporters

158
Q

Fibrinogen: (1)

A

Important for clotting

159
Q

Which hormone stimulates bicarbonate secretion from the pancreas into the SI?

A

Secretin

160
Q

What is able to cross the basolateral membrane of enterocytes?

A

Free Amino Acids ONLY

161
Q

Human genome protein-coding genes are ___% enzymes

A

16%

162
Q

Biological Catalysts:

_______ Proteins: (3)

A

GLOBULAR Proteins:
Speed up reactions with being consumed
Do not shift equilibrium, just reach it faster
Very specific

163
Q

Cofactor: (definition)

  • (4 examples)
  • (category)
A

Cofactor: INorganic components need to work.

  • Fe, Mg, Zn, Se
  • Minerals
164
Q

Coenzyme: (definition)

  • Often used to…
  • (7 examples)
  • (category)
A

Coenzyme: Organic component needed to work

  • Often used to TRANSFER CHEMICAL GROUPS
  • Vit. B6, Vit. B12, Thiamin, Folate, Riboflavin, Biotin, Niacin
  • Vitamins
165
Q 
Cofactor : Enzyme(s)
Copper:
Iron:
Potassium:
Magnesium:
Zinc:
A

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
Q 
Coenzyme : Chemical Group Transferred
Biotin:
Pantothenic Acid:
B12
Riboflavin and Niacin:
Folate:
A 
Biotin: Carbon Dioxide
Pantothenic Acid: Acyl Groups (fatty acids)
B12: H atoms
Riboflavin and Niacin: Electrons
Folate: Methyl Groups
167
Q

________ - protein part of enzyme only
- Missing _________/________
________ - Complete (active) enzyme
- _______ + ________/_______

A

APOENZYME - protein part of enzyme only
- missing COFACTOR/COENZYME
HOLOENZYME - complete (active) enzyme
- PROTEIN + COFACTOR/COENZYME

168
Q

_______ - Enzyme precursor (inactive)

example

A

Zymogen

Trypsinogen –> Enterokinase –> Trypsin

169
Q

6 Classes of enzymes

A 
Oxidoreductase
Transferase
Isomerase
Hydrolase
Lyase
Ligase
170
Q

Oxidoreductase: (2)

A 
Addition or removal of H
Requires coenzyme (NAD and FAD)
171
Q

Transferase:

A

Transfer a functional group from one molecule to another

172
Q

Isomerase:

A

Rearrange functional group on one molecule

173
Q

Hydrolase: (2)

A

Causes HYDROLYSIS reaction

Water breaks bond

174
Q

Lyase:

A

Cleaves C-C, C-S or C-N bonds

175
Q

Ligase: (2)

A

JOINS bond between C and another element (O, S, N)

Generally need energy from ATP

176
Q 
Enzymes:
Reaction rate (speed) is dependant on \_\_\_\_\_\_\_\_ \_\_\_\_\_\_\_\_.
How does it impact reaction rate?
A

Activation Energy
Higher AE = SLOWER reaction
Lower AE = FASTER reaction

177
Q

How do catalysts work?

A

Catalysts speed up reactions by lowering the activation energy

178
Q

Enzymes contain an _____ _____ which reacts with specific _______

A

Active Site

Substrate

179
Q

Active Site: (2)

A

Binding Site: Holds substrate in proper place - weak, non-covalent interactions between AA and substrate
Catalytic Site: Where reaction actually occurs

180
Q

Vo =
Vmax =
Km =

A 
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
Q

Smaller Km =

A

High affinity to bind [S] (less [S] needed to reach 1/2 Vmax)

182
Q

Irreversible Inhibitor

A

Covalent Bonding

183
Q 
Reversible Inhibitor (1)
- (4 sub-points)
A

Non-Covalent Interactions

  • Can dissociate
  • Competitive
  • Uncompetitive
  • Noncompetitive
184
Q

With competitive inhibitor…

in relation to Vo, Km, Vmax

A

Changes Km

Does NOT change Vmax

185
Q

With uncompetitive inhibitor…

in relation to Vo, Km, Vmax

A

Both Km and Vmax change

186
Q

With noncompetitive inhibitor…

(in relation to Vo, Km, Vmax

A

Changes Vmax

Does NOT change Km

187
Q

___% of the most commonly prescribed drugs target and inhibit enzymes

A

50%

188
Q

Antibiotics inhibit enzymes that make…

A

Proteins for their cell wall

189
Q

Enzymes in a pathway that are easier to control.

A

Regulatory Enzymes

190
Q

Common covalent modifying groups: (4)

A

Phosphates —> Serine, Threonine, Tyrosine
Adenine —> Tyrosine ONLY
Acetyl —> Lysine ONLY
Methyl —> Glutamate ONLY

191
Q

Phosphorylation:

A

Adding or removing phosphate group to serine, threonine or tyrosine

192
Q

Phosphorylation of glycogen _________ increases activity.

A

Phosphorylase

193
Q

Phosphorylation of glycogen ________ decreases activity

A

Synthase

194
Q

Cells can regulate the amount of E by…

A

Induction or Repression

195
Q

Inductions occurs from…

A

Hormones and Diet

Biochemistry 1 (5 decks)

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