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Biochemistry > V - Proteins > Flashcards

V - Proteins Flashcards

1
Q

Most abundant and functionally diverse molecules in living systems

A

proteins

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2
Q

Linear polymers if amino acids

A

proteins

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3
Q

Set of all the proteins expressed by an individual cell at a particular time

A

proteome

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4
Q

Aims to identify the entire complement of proteins elaborated by a cell under diverse conditions

A

Proteomics

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5
Q

Aims to identify proteins and their post-translational modifications whose appearance or disappearance correlates with physiologic phenomena, aging or specific diseases

A

Proteomics

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6
Q

There are more than 300 amino acids but only ___ are commonly found in mammalian proteins,

A

20

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7
Q

All amino acids have _____, _____ & _____ except for _____.

A

carboxyl group (-COOH), amino group (-NH2), unique side chain (R-group), proline

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8
Q

All three molecular groups in an amino acid are bonded to a central

A

α-carbon

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9
Q

Dictates the function of the amino acid in a protein

A

R-group

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10
Q

Amino Acids: Alipathic Side Chains

A

Glycine, Alanine, Valine, Leucine, Isoleucine

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11
Q

Amino Acids: Hydroxylic Groups

A

Serine, Threonine, Tyrosine

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12
Q

Amino Acids: Sulfur Atoms

A

Cysteine, Methionine

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13
Q

Amino Acids: Aromatic Side Chains

A

Histidine, Phenylalanine, Tyrosine, Tryptophan

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14
Q

Imino Acid

A

Proline

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15
Q

Amino Acids: Basic Groups

A

Lysine, Arginine, Histidine

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16
Q

Amino Acids: Acidic Groups

A

Aspartic acid, Asparagine, Glutamic acid, Glutamine

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17
Q

Side Chains: net charge of zero at physiologic pH, promote hydrophobic interactions, cluster in the interior of the protein

A

non-polar side chains

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18
Q

Amino Acids: has the smallest side chain, used in the first step of heme synthesis, used in purine synthesis, major inhibitory neurotransmitter in the spinal cord

A

Glycine

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19
Q

Glycine + Succinyl CoA

A

δ-ALA (aminolevulinic acid)

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20
Q

Amino Acids: Amino Acids: Carries nitrogen from peripheral tissues to the liver

A

Alanine

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21
Q

Amino Acids: branched-chain amino acids whose metabolites accumulate in Maple Syrup Urine Disease (deficiency in branched-chain α-ketoacid dehydrogenase)

A

Valine, Isoleucine, Leucine

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22
Q

Amino Acids: accumulates in Phenylketonuria

A

Phenylalanine

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23
Q

Deficient enzyme in PKU

A

Phenylalanine Hydroxylase

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24
Q

Accumulating metabolites in PKU

A

phenyllactate, phenylpyruvate, phenylacetate

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25
Q

Causes the musty odor in PKU

A

phenylacetate

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26
Q

Amino Acids: has the largest side chain, precursor for niacin, serotonin (5-HT) and melatonin

A

Tryptophan

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27
Q

Amino Acids: precursor of homocysteine

A

Methionine

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28
Q

Methionine is used in transfer of methyl groups as

A

S-adenosylmethionine (SAM)

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29
Q

Amino Acids: contributes to the fibrous structure of collagen and interrupts α-helices in globular proteins

A

Proline

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30
Q

Side Chains: zero net charge at physiologic pH, presence of side chains that can participate in hydrogen bonds

A

uncharged polar side chains

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31
Q

Amino Acids: contains a sulfhydryl group that is an active part of many enzymes

A

Cysteine

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32
Q

2 cysteine molecules connected by a covalent disulfide bond, abundant in keratin

A

Cystine

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33
Q

Products from Phenylalanine

A

Phenylalanine → Tyrosine → L-Dopa → Dopamine → Norepinephrine → Epinephrine

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34
Q

Precursor for thyroxine and melanin

A

Tyrosine

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35
Q

Amino Acids: phosphorylation site of enzyme modification, linked to carbohydrate groups in glycoproteins

A

Serine

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36
Q

Amino Acids: sites for O-linked glycosylation in the golgi apparatus

A

Serine, Threonine

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37
Q

Amino Acids: have a carbonyl group and an amide group that can also form hydrogen bonds

A

Asparagine, Glutamine

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38
Q

Amino Acids: site for N-linked glycosylation in the endoplasmic reticulum

A

Asparagine

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39
Q

Amino Acids: deaminated by glutaminase resulting in the formation of ammonia, major carrier of nitrogen to the liver from the peripheral tissues

A

Glutamine

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40
Q

Side Chains: negatively charged at physiologic pH because of the carboxylate group, participate in ionic reactions

A

acidic side chains

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41
Q

Amino Acids: precursor for GABA and glutathione

A

Glutamate

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42
Q

Side Chains: positively charged because of the amine group

A

basic side chains

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43
Q

At neutral pH, arginine and lysine are

A

positively charged

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44
Q

At neutral pH, histidine is

A

neutral (weak base)

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45
Q

Amino Acids: precursor of histamine, used in the diagnosis of folic acid deficiency

A

Histidine

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46
Q

Ingividuals deficient in folic acid excrete increased amounts of FIGlu in urine particularly after ingestion of large doses of histidine

A

N-formiminoglutamate Excretion Test

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47
Q

Amino Acids: precursor of creatinine, urea and nitric oxide

A

Arginine

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48
Q

21st Amino Acid

A

Selenocysteine

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49
Q

Amino Acids: found in a handful of proteins, including certain peroxidases and reductases, inserted into polypeptides during translation but is not specified by a simple three-letter codon, a selenium atom replaces the sulfur in cysteine

A

Selenocysteine

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50
Q

Non-Polar Amino Acids

A

Glycine, Alanine, Leucine, Isoleucine, Valine, Phenylalanine, Tryptophan, Methionine, Proline

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51
Q

Polar Uncharged Amino Acids

A

-OH (Serine, Threonine, Tyrosine), -SH (Cysteine), Amide (Asparagine, Glutamine)

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52
Q

Charged Amino Acids

A

Acidic (Aspatrate, Glutamate), Basic (Lysine, Arginine, Histidine)

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53
Q

All amino acids are chiral except for

A

Glycine

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54
Q

An atom in a molecule that is bonded to 4 different chemical species allowing for optical isomerism

A

chiral center

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55
Q

Molecuels that are exact mirror images of each other

A

Stereoisomers/Enentiomers/Optical Isomers

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56
Q

Most common configuration of AAs

A

L-configuration

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57
Q

A chemical compound that has a total net charge of zero

A

Zwitterion

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58
Q

pH where the zwitterion predominates (AA is uncharged)

A

Isoelectric Point (pI)

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59
Q

Isoelectric Point (pI)

A

(pKa before + pKa after)/2

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60
Q

Molecular group that accepts protons

A

amino group

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61
Q

Molecular group that donates protons

A

carboxylic acid group

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62
Q

AAs that cannot be synthesized by the body and must come from the diet

A

Phenylalanine, Valine, Tryptophan, Threonine, Histidine, Arginine, Leucine, Lysine

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63
Q

Conditionally Non-Essential AAs: may be made in the body but usually not enough

A

Arginine

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64
Q

Conditionally Non-Essential AAs: may be recycled but should eventually be consumed since it is not made at all

A

Histidine

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65
Q

Linear sequence of a protein’s amino acids

A

Primary Structure

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66
Q

Attaches α-amino group of ne AA to the α-carbonyl group of another, very stable, can only be disrupted by hydrolysis through prolonged exposure to a strong acid or base at elevated temperatures, polar, can form hydrogen bonds

A

Peptide Bonds

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67
Q

Makes the peptide bond rigid and planar

A

partial double bond

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68
Q

Cleaves the N-terminal amino acid

A

Sanger’s reagent, Edman’s reagent

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69
Q

Cleaves the C-terminal amino acid

A

Hydrazine, Carboxypeptidase

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70
Q

Used to detect covalent modifications in proteins

A

mass spectrometry

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71
Q

The folding of short (3-30 residues) contiguous segments of polypeptide into geometrically ordered units, regular arrangements of AA that are located near each other in the linear sequence, stabilized by excessive hydrogen bonding

A

Secondary Structure

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72
Q

Secondary Structures: most common, R-handed spiral with polypeptide back bone core, side chains extend outward, 3.6 AA per turn of the spiral

A

Alpha Helix

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73
Q

Alpha helices are disrupted by

A

proline, large R-groups, charged R-groups

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74
Q

Secondary Structures: surfaces appear flat and pleated, 2 or more peptide chains parallel to each other, interchain and intrachain bonds

A

Beta Sheet

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75
Q

Secondary Structures: combinations of adjacent secondary structures such as β-α-β unit, Greek key, β-meander, β-barrel

A

Motifs (Supersecondary Structures)

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76
Q

Secondary Structures: R-handed spiral, H-bonds parallel to helix, keratin, hemoglobin

A

Alpha Helix

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77
Q

Secondary Structures: sheets, H-bonds perpendicular to sheets, amyloid, immunoglobulin

A

Beta-Pleated Sheet

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78
Q

Overall 3D shape of the protein, globular, fibrous, refers to the folding of domains and their final arrangement in the polypeptide

A

Tertiary Structure

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79
Q

The tertiary structure of proteins are stabilized by

A

disulfide bonds, hydrophobic interactions, hydrogen bonds, ionic bonds

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80
Q

Fundamental functional and 3D structural units of a polypeptide, formed by combinations of motifs

A

Domains

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81
Q

Specialized group of group of proteins required for the proper folding of many species of proteins, prevent aggregation, thus providing an opportunity for the formation of appropriate secondary structural elements and their subsequent coalescence into a molten globule

A

Chaperones

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82
Q

Can rescue proteins that have become thermodynamically trapped in a misfolded dead end by unfolding hydrophobic regions

A

Chaperones

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83
Q

Structure of proteins consisting of more than one polypeptide chain, held together by non-covalent bonds

A

Quarternary Structure

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84
Q

Precipitation of a protein so that it forms ordered crystals that can diffract x-rays

A

X-ray Crystallography

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85
Q

Measures the absorbency of radiofrequency electromagnetic energy by certain atomic nuclei, groups of nuclei have particular absorbency patterns

A

Nuclear Magnetic Resonance Spectroscopy

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86
Q

Molecular dynamics programs can be used to stimulate the conformational dynamics of a protein and the manner in which factors such as temerature, pH, ionic strongth or AA amino acid substitutions influence these motions

A

Molecular Modeling

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87
Q

Disruption of a protein’s structure

A

Denaturation

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88
Q

Means of Protein Denaturation

A

heat, organic solvents, mechanical mixing, strong acids or bases, detergents, ions of heavy metals (lead & mercury)

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89
Q

Fatal neurodegenerative diseases characterized by spongiform changes, astrocytic gliomas and neuronal loss resulting from the deposition of insoluble protein aggregates in neural cells

A

Prion Diseases

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90
Q

Prions: normal protein, rich in α-helices

A

PrPc

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91
Q

Prions: pathologic conformation, rich in β-sheets

A

PrPsc

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92
Q

The caharcteristic senile plaques and neurofibrillary bundles of the protein β-amyloid which undergoes conformational transformation from a soluble α-helix rich state rich in β-sheets and prone ti self aggregation, mediated by Apo-E

A

Alzheimer’s Disease

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93
Q

A complex of protoporphyrin IX and ferrous iron (Fe2+), electron carrier in cytochromes, active site of the enzyme catalase that breaks down hydrogen peroxide, reversibly binds oxygen in myoglobin and hemoglobin

A

Heme

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94
Q

Heme protein found exclusively in red blood cells, composed of heme and 4 globin chains

A

Hemoglobin

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95
Q

Major transporter of CO2 in the blood

A

HCO3 (75%), carbaminohemoglobin (25%)

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96
Q

Hemoglobin: ζ2ε2, conception until the first few months, yolk sac

A

Embryonal Hemoglobin (Gower 1)

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97
Q

Hemoglobin: α2γ2, first few months to after birth, liver

A

Fetal Hemoglobin (HbF)

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98
Q

Hemoglobin: α2γ2, 8th month onwards, marrow

A

Hemoglobin A (HbA)

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99
Q

Hemoglobin: α2δ2, shortly after birth onwards, marrow

A

Hemoglobin A2 (HbA2)

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100
Q

Binds up to 4 molecules of oxygen, exhibits positive cooperativity, sigmoidal curve

A

Hemoglobin

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101
Q

Hemoglobin binds to O2 with increasing affinity

A

Positive Cooperativity

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102
Q

Hemoglobin: low oxygen affunity

A

T (taut)

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103
Q

Hemoglobin: high oxygen affinity (300x)

A

R (relaxed)

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104
Q

Heme protein found in the heart and skeletal muscles, reservoir of oxygen, oxygen carrier that increases the rate of transport of O2 within the muscle cell, hyperbolic curve

A

Myoglobin

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105
Q

Consists of a single polypeptide chain composed of polar and non-polar AAs, contains histidine for O2 binding, released from damaged muscle fibers and turns the urine dark red, can be detected in plasma following MI

A

Myoglobin

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106
Q

O2 Carriers: 1 polypeptide

A

Myoglobin

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107
Q

O2 Carriers: carries 1 O2

A

Myoglobin

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108
Q

O2 Carriers: hyperbolic curve (saturation)

A

Myoglobin

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109
Q

O2 Carriers: storage

A

Myoglobin

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110
Q

O2 Carriers: heart, muscle

A

Myoglobin

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111
Q

O2 Carriers: 4 polypeptides

A

Hemoglobin

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112
Q

O2 Carriers: carries 4 O2

A

Hemoglobin

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113
Q

O2 Carriers: sigmoidal curve (cooperativity)

A

Hemoglobin

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114
Q

O2 Carriers: transport

A

Hemoglobin

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115
Q

O2 Carriers: allosteric effects are present

A

Hemoglobin

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116
Q

Factors whose interaction with one site of the hemoglobin affects the binding of oxygen to heme groups at other locations, effect may be positive or negative, myoglobin is not affected

A

Allosteric Effectors

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117
Q

Shifts the O2 Dissociation Curve to the right

A

CO2, acidity, 2,3-BPG, exercise, temperature

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118
Q

The deoxy form of hemoglobin has a greater affinity for protons than does oxyhemoglobin

A

Bohr Effect

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119
Q

Stabilizes the T structure of hemoglobin by forming additional salt bridges that must be broken prior to conversion to the R state, synthesized by erythrocytes

A

2,3-BPG

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120
Q

Oxidized form of Hgb (Fe3+) that does not bind to O2 as readily but has a high affinity for CN, cyanosis, anxiety, headache, dyspnea, chocolate cyanosis (muddy brown), 85% O2 Sat.

A

Methemoglobin

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121
Q

Hgb bound to carbon monoxide instead of O2, cherry pink

A

Carboxyhemoglobin

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122
Q

Hemoglobin: CO

A

Carbohyhemoglobin

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123
Q

Hemoglobin: CO2

A

Carbaminohemoglobin

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124
Q

Hemoglobin: cherry pink

A

Carboxyhemoglobin

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125
Q

Hemoglobin: muddy brown

A

Methemoglobin

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126
Q

Hemoglobin: When blood glucose enters erythrocytes, it glycosylates the

A

ε-amino group of lysine residues and the amino terminals of hemoglobin (HbA1c)

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127
Q

Disorder characterized by an inherited (intrinsic) defect in the RBC membrane that renders erythrocytes spheroidal, less deformable and vulnerable to splenic sequestration and destruction

A

Hereditary Spherocytosis

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128
Q

Hereditary Spherocytosis: Mutations

A

spectrin, band 4.1, band 3

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129
Q

Hereditary Spherocytosis: Diagnosis

A

osmotic fragility test

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130
Q

Hereditary Spherocytosis: Treatment

A

splenectomy for symptomatic patients

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131
Q

Point mutation in both genes coding for β-chain that results in a valine rather than a glutamate, homozygous recessive disorder

A

Sickle Cell Disease

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132
Q

Polymerization and decreased solubility of the deoxy form of Hgb, distortion of the RBC membrane, misshapen, rigid RBCs occlude capillaries

A

Sickle Cell Disease

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133
Q

Amenia, tissue anoxia, painful crises, protective against malaria

A

Sickle Cell Disease

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134
Q

Sickle Cell Disease: Treatment

A

hydration, analgesics, antibiotics if with infection, transfusions, hydroxyurea

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135
Q

Hemoglobin variant that has a single amino acid substitution in the 6th position of the β-chain in which lysine is substituted for glutamate, homzygous patients present with mild hemolytic anemia

A

Hemoglobin C

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136
Q

Inadequate synthesis of the α-chains, leads to anemia due to β-chain accumulation and precipitation, symptoms appear at birth because α-chains are needed for HbF and HbA

A

Alpha Thalassemia

137
Q

Alpha Thalassemia: 1 defective gene

A

silent carrier

138
Q

Alpha Thalassemia: 2 defective genes

A

Alpha Thalassemia Trait

139
Q

Alpha Thalassemia: 3 defective genes

A

Hb H DIsease

140
Q

Alpha Thalassemia: 4 defective genes

A

Hydrops Fetalis

141
Q

Alpha Thalassemia: Chromosome

A

Chrom. 16

142
Q

Inadequate synthesis of β-chains, leads to anemia, accumulation of Hb Barts, α-chain precipitation, symptoms appear after birth sins Hbf does not have β-chains

A

Beta Thalassemia

143
Q

Beta Thalassemia: 1 defective gene

A

Beta Thalassemia Minor

144
Q

Beta Thalassemia: 2 defective gene

A

Beta Thalassemia Major

145
Q

MOst abundant protein in the body, long stiff extracellular structure in which 3 polypeptides (α-chain) each 1000 AA in length are wound around one another in a triple helix, stabilized by hydrogen bonds, 28 distinct types made up of 30 distinct polypeptide chains

A

Collagen

146
Q

Most Common Collagen Type

A

Type 1

147
Q

Collagen is rich in

A

Glycine, Proline

148
Q

X portion of collagen

A

Proline (facilitates kinking)

149
Q

Y portion of collagen

A

hydroxyproline or hydroxylisine

150
Q

Formed in fibroblasts or in the osteoblasts of bone and chondroblasts of cartilage, secreted into the extracellular matrix

A

Collagen

151
Q

Collagen monomers aggregate and become cross-linked to form

A

Collagen Fibrils

152
Q

Collagen: pro α-chain + signal peptide

A

PrePro α-chain

153
Q

Collagen: signal peptide removed

A

Pro α-chain

154
Q

Collagen: lysine and proline are hydroxylated

A

Procollagen

155
Q

Collagen: 3 procollagen chains form the triple helix

A

Triple Helix Procollagen

156
Q

Collagen: secreted from the cell

A

Triple Helix

157
Q

Collagen: triple helix with propeptide removed

A

Tropocollagen

158
Q

Collagen: lysine cross-links, parallel, staggered

A

Collagen Fibrils

159
Q

Collagen: bone

A

I

160
Q

Collagen: skin

A

I

161
Q

Collagen: tendon

A

I

162
Q

Collagen: dentin

A

I

163
Q

Collagen: fascia

A

I

164
Q

Collagen: cornea

A

I

165
Q

Collagen: late wound repair

A

I

166
Q

Collagen: cartilage

A

II

167
Q

Collagen: vitreous body

A

II

168
Q

Collagen: nucleus pulposus

A

II

169
Q

Collagen: skin

A

III

170
Q

Collagen: blood vessels

A

III

171
Q

Collagen: uterus

A

III

172
Q

Collagen: fetal tissue

A

III

173
Q

Collagen: granulation tissue

A

III

174
Q

Collagen: basement membrane/basal lamina

A

IV

175
Q

Results from inheritable defects in the metabolism of fibrillar collagen, collagen is most frequently affected

A

Ehlers-Danlos Syndrome

176
Q

Hyperextensible skin, tendency to bleed, hypermobile joints, high risk for berry aneurysms

A

Ehlers-Danlos Syndrome

177
Q

Brittle bone syndrome, mutation in collagen genes result to bones that easily bend and fracture, most common form is autosomal dominant with abnormal collagen type

A

Osteogenesis Imperfecta

178
Q

Multiple fractures, blue sclerae, hearing loss, dental imperfections

A

Osteogenesis Imperfecta

179
Q

Hydroxylation of collagen is a post-translational modification requirin ascorbic acid. deficiency causes decreased cross-linking of collagen fibers

A

Scurvy

180
Q

Sore spongy gums, loose teeth, poor wound healing, petechiae on skin and mucous membranes

A

Scurvy

181
Q

A number of genetic disorders affecting the structure of type IV collagen fibers, the major collagen found in the basement membranes of the renal glomeruli, hematuria, ESRD

A

Alport’s Syndrome

182
Q

Kinky hair, growth retardation, reflects a dietary deficiency of the copper required by lysyl oxidase which catalyzes a key step in formation of the covalent cross-links that strengthen collagen fibers

A

Menke’s Syndrome

183
Q

The skin breaks and blisters as a result of minor trauma, the dystrophic form is due to mutations affecting the structure of type VII collagen which forms delicate fibrils that anchor the basal lamina to collagen fibrils in the dermis

A

Epidermolysis Bullosa Dystrophica

184
Q

Connective tissue protein with rubber-like properties, responsible for extensibility and elastic recoil in tissues

A

Elastin

185
Q

Rich in proline and lysine but little hydroxyproline and no hydroxylysine

A

Elastin

186
Q

Precursor tropoelastin is deposited into an irregular fibrillin scaffold cross-linked by desmosine

A

Elastin

187
Q

Elastin is found in tissues where elastic recoil is needed like in

A

lungs, large arteries, elastic ligaments, vocal cords, ligamentum flavum

188
Q

Autosomal dominant connective tissue disorder, mutation in fibrillin gene

A

Marfan Syndrome

189
Q

Taller, thinner, dolichostenomelia, arachnodactyly, ascending aortic dilatation and dissection

A

Marfan Syndrome

190
Q

Deficiency in the enzyme that inhibits proteolytic enzymes from hydrolyzing and destroying proteins, elastase destroys the alveolar walls resulting in emphysema

A

α1 Trypsin Deficiency

191
Q

Many different genetic types, triple helix, (Gly-X-Y)n repeating structure, presence of hydroxylysine, carbohydrate containing, intramolecular aldol cross-links, presence of extension peptides during biosynthesis

A

Collagen

192
Q

One genetic type, Intramolecular desmosine cross-links

A

Elastin

193
Q

Net accumulation of proteins as in growth & pregnancy

A

Positive Nitrogen Balance

194
Q

Net breakdown of protein as in surgery, advanced cancer, kwashiorkor or marasmus, starvation

A

Negative Nitrogen Balance

195
Q

Protein Turnover per day

A

300-400g/day

196
Q

Energy-dependent protein degradation mechanism

A

Ubiquitin-Proteasome Mechanism

197
Q

Protein Degradation: Endogenous

A

Proteasome

198
Q

Protein Degradation: Exogenous

A

Lysosome

199
Q

Sum of all free AAs in cells and ECF, degradation and turnover of body protein, dietary intake, synthesis of non-essential AAs

A

Amino Acid Pool

200
Q

Resorption of Proteins per day

A

150g/day

201
Q

Degradation of Proteins per day

A

50-100g/day

202
Q

Protein Digestion: Stomach

A

HCl, Pepsin

203
Q

Protein Digestion: Pancreatic Enzymes

A

Zymogens activated by Trypsin

204
Q

Protein Digestion: liberate AAs and dipeptides

A

Aminopeptidases

205
Q

Protein Digestion: absorbed by secondary active transport

A

Free AAs

206
Q

Protein Digestion: Endopeptidases

A

Trypsin, Chymotrypsin, Elastase

207
Q

Protein Digestion: Exopeptidases

A

Carboxypeptidase, Aminopeptidase

208
Q

HCl is produced by

A

parietal cells

209
Q

Pepsinogen is produced by

A

chief cells

210
Q

AA Catabolism: removal of the α-amino group (deamination) forming ammonia and a corresponding α-ketoacid

A

First Phase

211
Q

AA Catabolism: carbon skeletons of α-ketoacids are converted to common intermediates of energy-producing metabolic pathways (Glycolysis, Krebs Cycle)

A

Second Phase

212
Q

Major disposal form of nitrogen

A

Urea

213
Q

Nitrogen Excretion: seen in telostean fish, excrete highly toxic ammonia

A

Ammonotelic

214
Q

Nitrogen Excretion: land animals, humans, non-toxic water-soluble urea

A

Ureotelic

215
Q

Nitrogen Excretion: birds, secrete uric acid as semisolid guano

A

Uricotelic

216
Q

Main steps in removing nitrogen from AA

A

transamination, oxidative deamination

217
Q

AA Nitrogen Removal: occurs in all cells of the body, all AAs must transfer their amino groups to α-ketoglutarate to form glutamate (except lysine & threonine)

A

Transamination

218
Q

Aminotransferases

A

Alanine Aminotransferase (ALT), Aspartate Aminotransferas (AST)

219
Q

Aminotransferases: Co-Enzyme

A

Pyridoxal Phosphate (B6)

220
Q

ALT is also known as

A

SGPT (serum glutamate:pyruvate transferase)

221
Q

ALT/SGPT transaminates

A

pyruvate, alanine

222
Q

AST is also known as

A

SGOT (serum glutamate:OAA transferase)

223
Q

AST/SGOT transaminates

A

aspartate, OAA

224
Q

AA Nitrogen Removal: occurs in the liver and kidney, only for glutamate, glutamate is oxidized and deaminated to yield free ammonia (NH3) which is used to make urea

A

Oxidative Deamination

225
Q

Oxidative Deamination: Enzyme

A

Glutamate Dehydrogenase

226
Q

Peripheral Nitrogen Removal: synthesized from glutamate and ammonia, occurs in most tissues, including muscle

A

Glutamine

227
Q

Peripheral Nitrogen Removal: excess nitrogen from the peripheral tissues can reach the liver through transamination of pyruvate, occurs in muscle

A

Alanina

228
Q

In the liver, alanine is converted back to pyruvate which may undergo gluconeogenesis which can be transported back to the muscles

A

Glucose, Alanine Cycle

229
Q

Deaminates glutamine to produce ammonium ion (NH$+) which is excreted from the body, eliminates ammonium ion in the urine (kidneys), ammonium ion sent to the liver via the portal circulation for the urea cycle (SI)

A

Glutaminase

230
Q

Krebs-Henseleit Cycle/Ornithine Cycle

A

Urea Cycle

231
Q

Pathway for removal of nitrogenous waste products in the body, present only in the liver, major disposal of amino groups

A

Urea Cycle

232
Q

Donors of the atoms of urea

A

NH3 from free ammonia and aspartate, C from CO2

233
Q

Urea Cycle: only _____ can penetrate the mitochondrial membrane

A

Citrulline

234
Q

Urea Cycle

A

Ornithine + Carbamoyl Phosphate → Citrulline + Aspartate → Argininosuccinate - Fumarate → Arginine → Urea + Ornithine

235
Q

Urea Cycle: Mitochondrial Reactions

A

Formation of Carbamoyl Phosphate and Citrulline

236
Q

Urea Cycle: Cytoplasmic Reactions

A

Synthesis of Arginosuccinate, Cleavage of Arginosuccinate to form Arginine, Arginine cleavage into Urea and Ornithine

237
Q

Urea Cycle Enzymes: Formation of Carbamoyl Phosphate

A

Carbamoyl Phosphate Synthetase I

238
Q

Urea Cycle Enzymes: Formation of Citrulline

A

Ornithine Transcarbamoylase

239
Q

Urea Cycle Enzymes: Synthesis of Arginosuccinate

A

Arginosuccinate Synthetase

240
Q

Urea Cycle Enzymes: Cleavage of Arginosuccinate to form Arginine

A

Argininosuccinase

241
Q

Urea Cycle Enzymes: Arginine cleavage into Urea and Ornithine

A

Arginase

242
Q

Urea Cycle: Substrates

A

NH3, Aspartate, CO2

243
Q

Urea Cycle: Rate-Limiting Step

A

CO2 + NH3 → Carbamoyl Phosphate

244
Q

Urea Cycle: Rate-Limiting Enzyme

A

Carbamoyl Phosphate Synthetase I

245
Q

Urea Cycle: Energy Requirement

A

4 ATP

246
Q

Urea Cycle: Co-Factors

A

N-acetylglutamate, Biotin

247
Q

Diffuses from the liver and is transported in the blood to the kidneys where it is filtered and excreted in the urine, a portion diffuses from the blood into the intestines and is cleaved to CO2 and NH3 by bacterial urease

A

Urea

248
Q

Enzyme defect in the urea cycle, hyperammonemia, elevated blood glutamine, decreased BUN, lethargy, vomiting, hyperventilation, convulsions, cerebral edema, coma, death

A

Hereditary Hyperammonemia

249
Q

Hereditary Hyperammonemia: Type 1 Defect

A

Carbamoyl Phosphate Synthetase I Deficiency

250
Q

Hereditary Hyperammonemia: Type 2 Defect

A

Ornithine Transcarbamoylase Deficiency

251
Q

Hereditary Hyperammonemia: Treatment

A

low protein diet, administration of Na benzoate or phenylpyruvate to capture and excrete excess nitrogen

252
Q

Compromised liver function, tremors, slurring of speech, somnolence, vomiting, cerebral edema, blurring of vision

A

Acquired Hyperammonemia

253
Q

Exclusively ketogenic AAs

A

Leucine, Lysine

254
Q

Ketogenic and Glucogenic AAs

A

Phenylalanine, Tyrosine, Tryptophan, Isoleucine

255
Q

Ketogenic AAs yield

A

acetoacetate, acetyl-CoA/acetoacetyl-CoA

256
Q

Glucogenic AAs yield

A

Pyruvate, intermediates of the Krebs Cycle

257
Q

AAs that enter the Krebs Cycle via α-ketoglutarate

A

Glutamine, Glutamate, Proline, Arginine, Histidine

258
Q

AAs that enter the Krebs Cycle via Pyruvate

A

Alanine, Serine, Glycine, Cysteine, Threonine, Tryptophan

259
Q

AAs that enter the Krebs Cycle via Fumarate

A

Phenylalanine, Tyrosine

260
Q

AAs that enter the Krebs Cycle via Succinyl-CoA

A

Methionine, Valine, Isoleucine, Threonine

261
Q

AAs that enter the Krebs Cycle via Oxaloacetate

A

Aspartate, Asparagine

262
Q

AAs synthesized from transamination of α-ketoacids

A

Alanine, Aspartate, Glutamate

263
Q

AAs synthesized from amidation of Glutamate and Aspartate

A

Glutamine, Asparagine

264
Q

AA synthesized from Glutamate

A

Proline

265
Q

AA synthesized from Methionine and Serine

A

Cysteine

266
Q

AA synthesized from 3-phosphoglycerate

A

Serine

267
Q

AA synthesized from Serine

A

Glycine

268
Q

AA synthesized from Phenylalanine

A

Tyrosine

269
Q

AA synthesized into heme, purines, creatine, conjugated to bile acids

A

Glycine

270
Q

AA synthesized into phospholipid, sphingolipid, purines, thymine

A

Serine

271
Q

AA synthesized into GABA

A

Glutamate

272
Q

AA synthesized into thioethanolamine of CoA, taurine

A

Cysteine

273
Q

AA synthesized into histamine

A

Histidine

274
Q

AA synthesized into creatinine, polyamines, NO

A

Arginine

275
Q

AA synthesized into serotonin, NAD, NADP, melatonin

A

Tryptophan

276
Q

AA synthesized into catecholamine, thyroid hormones (T3 & T4), melanin

A

Tyrosine

277
Q

Deficiency in phenylalanine hydroxylase or tetrahydrobiopterine cofactor, tyrosine becomes essential, phenylalanine builds up, excess phenylketones (phenylacetate, phenyllactate, phenylpyruvate)

A

Phenylketonuria

278
Q

Mental retardation, growth retardation, fair skin, eczema, musty body odor

A

Phenylketonuria

279
Q

Phenylketonuria: Treatment

A

decrease phynylalanine and increase tyrosine in diet

280
Q

Congenital deficiency of homogentistic acid oxidase in the degradative pathway of tyrosine, alkapton bodies cause urine to turn to black on standing, connective tissue is dark (ochronosis), benign, may have debilitating arthralgias, pigmentation of the sclera (Osler’s Sign)

A

Alkaptonuria

281
Q

Congenital deficiency in Tyrosinase or Tyrosine Transporters, lack of melanin leads to increased risk of skin cancer, can result from a lack of migration of neural crest cells

A

Albinism

282
Q

Albinism: inability to synthesize melanin from tyrosine, autosomal recessive

A

Tyrosinase Deficiency

283
Q

Albinism: decreased amounts of tyrosine and thus melanin

A

Defective Tyrosine Transporters

284
Q

Autosomal recessive, cystathionine synthase deficiency, decreased affinity of cystathione synthase for pyridoxal phosphate, homocysteine methyltransferase deficiency, excess homocysteine, cysteine becomes essential

A

Homocystinuria

285
Q

Treatment for cystathionine synthase deficiency

A

decrease methionine, increase cysteine, B6 and folate in the diet

286
Q

Treatment for decreased affinity of cystathione synthase for pyridoxal phosphate

A

increase B6 in the diet

287
Q

Mental retardation, osteoporosis, tall, kyphosis, lens subluxation (downward, inward), atherosclerosis, stroke, MI

A

Homocystinuria

288
Q

Common inherited defect of renal tubular AA transporter for cystine, ornithine, lysine and arginine in the PCT of the kidneys, excess cystine in the urine leads to cystine stones (staghorn calculi)

A

Cystinuria

289
Q

Cystinuria: Treatment

A

Acetazolamide (alkalinize the urine)

290
Q

Kidney Stones in Acidic Urine

A

uric acid, cystine

291
Q

Kidney Stones in Alkaline Urine

A

magnesium alkaline phosphate (struvite) from urease producing bacteria (Proteus)

292
Q

Blocked degradation of branched AA (Valine, Isoleucine, Leucine) due to a deficiency in α-ketoacid dehydrogenase, causes increased α-ketoacid in the blood (esp. leucine), severe CNS defects, mental retardation, death

A

Maple Syrup Urine Disease

293
Q

Cyclic compounds formed from the linkage of four pyrrole rings through methyne (-HC) bridges, form complexes with metal ions bound to nitrogen atom of the pyrrole rings

A

Porphyrins

294
Q

The heme of hemoglobin contains

A

iron

295
Q

The heme of chlorophyll contains

A

magnesium

296
Q

Heme synthesis is present in

A

all tissues

297
Q

Used in hemoglobin, myoglobin, cytochromes, catalase, peroxidase, guanylate cyclase

A

heme

298
Q

The initial and the last three steps in the formation of porphyrins occur in

A

mitochondria

299
Q

The intermediate steps occur in the

A

cytosol

300
Q

Steps in Heme Synthesis

A

Formation of δ-aminolevulinic acid, porphobilinogen, uroporphobilinogen, heme

301
Q

Heme Synthesis: Rate-Limiting Step

A

Glycine + Succinyl CoA → δ-Aminolevulinic Acid

302
Q

Heme Synthesis: Rate-Limiting Enzyme

A

ALA Synthase

303
Q

Heme Synthesis: ALA Synthase Co-Factor

A

Pyridoxine (B6)

304
Q

Heme Synthesis: condensation of two molecules of ALA by zinc-containing ALA Dehydratase, inhibited by heavy metal ions (lead) that replace the zinc

A

Formation of Porphobilinogen

305
Q

Introduction of iron (Fe3+) into protoporphyrin IX occurs spontaneously but the rate is enhanced by ferrochelatase, also inhibited by lead

A

Formation of Heme

306
Q

Genetic or acquired disorders due to abnormalities in the pathway of biosynthesis of heme, erythropoietic or hepatic

A

Porphyrias

307
Q

Most Common Porphyria

A

Porphyria Cutanea Tarda

308
Q

Photosensitivity or chronic inflammation to overt blistering and shearing in sun-exposed areas, abdominal pain (after ring, step 5 onwards), neuropsychiatric symptoms (before ring)

A

Porphyria

309
Q

Pyridoxine deficiency associated with Isoniazid therapy

A

Sideroblastic Anemia (ringed sideroblasts)

310
Q

Heme synthase (ferrochelatase) introduces the Fe2+ into protoporphyrin IX to make the heme ring, microcytic, hypochromic anemia

A

Iron Deficiency

311
Q

Inactivates many enzymes in heme synthesis (ALA dehydratase, ferrochelatase)

A

Lead Poisoning

312
Q

Coarse basophilic stippling of RBC, headache, memory loss, peripheral neuropathy, claw hand, wrist-drop, nausea, abdominal pain, diarrhea, lead lines in gums, deposits in epiphyses, increase urinary ALA and free erythrocyte porphyrin

A

Lead Poisoning

313
Q

Causes microcytic, hypochromic anemia

A

IDA, Thalassemia, Lead Poisoning

314
Q

Causes megaloblastic anemia

A

Folate/B12 Deficiency, Pernicious Anemia

315
Q

Causes normocytic, normochromic anemia

A

blood loss, chronic disease, CKD

316
Q

Causes increased MCHC

A

Hereditary Spherocytosis

317
Q

ALA synthase deficiency, anemia, decreased red cell counts and Hgb

A

X-linked Sideroblastic Anemia

318
Q

Abdominal pain, neuropsychiatric, urinary δ-aminolevulinic acid

A

ALA Dehydratase Deficiency

319
Q

Uroporphyrinogen I synthase deficiency, abdominal pain, neuropsychiatric, urinary porphobilinogen (+), uroporphyrin (+)

A

Acute Intermittent Porphyria

320
Q

Uroporphyrinogen III synthase deficiency, no photosensitivity, urinary porphobilinogen (-), uroporphyrin (+)

A

Congenital Erythropoietic Porphyria

321
Q

Uroporphyrinogen decarboxylase deficiency, photosensitivity, urinary porphobilinogen (-), uroporphyrin (+)

A

Porphyria Cutanea Tarda

322
Q

Coproporphyrinogen oxidase deficiency, photosensitivity, abdominal pain, neuropsychiatric, urinary porphobilinogen (+), uroporphyrin (+), fecal protoporphyrin (+)

A

Hereditary Coproporphyria

323
Q

Protoporphyrinogen oxidase deficiency, photosensitivity, abdominal pain, neuropsychiatric, urinary porphobilinogen (+), fecal protoporphyrin (+)

A

Variegate Porphyria

324
Q

Ferrochelatase deficiency, photosensitivity, fecal protoporphyrin (+), red cell protoporphyrin (+)

A

Protoporphyria

325
Q

After 120 days, RBCs are taken up and degraded by the

A

reticuloendothelial system (liver, spleen)

326
Q

Heme Degradation

A

formation of bilirubin → uptake of bilirubin by the liver → formation of bilirubin diclucoronide → secretion of bilirubin into bile → formation of urobilins in the intestine

327
Q

Reactions of heme oxygenase in reticuloendothelial cells

A

heme → biliverdin (green) → bilirubin (red orange)

328
Q

Bilirubin transported to the liver by binding to

A

albumin

329
Q

In the liver, bilirubin binds to intracellular proteins particularly

A

ligandin

330
Q

Bilirubin is conjugated to two molecules of glucuronic acid by

A

Bilirubin Glucuronyltransferase

331
Q

Bilirubin Glucuronyltransferase Deficiency

A

Crigler-Najjar I and II, Gilbert Syndrome

332
Q

Transported into the bile canaliculi and then into the bile, susceptible to impairment in liver disease

A

Bilirubin Diglucuronide

333
Q

In the gut, bilirubin is converted into a colorless substance

A

urobilinogen

334
Q

Intestinal bacteria oxidize urobilinogen into

A

stercobilin (brown)

335
Q

Some urobilinogen is reabsorbed from the blood and enters the

A

portal circulation

336
Q

Remaining urobilinogen is transported by the blood to the kidney where it is converted to

A

urobilin (yellow)

337
Q

Jaundice: hemolytic anemias, neonatal physiologic jaundice, Crigler-Najjar I and II, Gilbert syndrome, toxic hyperbilirubinemia

A

Unconjugated Hyperbilirubinemia

338
Q

Jaundice: biliary tree obstruction, Dubin-Johnson syndrome, Rotor Syndrome

A

Conjugated Hyperbilirubinemia

339
Q

Used to measure total and direct bilirubin

A

Van den Bergh Reaction

Biochemistry (14 decks)

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