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212 Cards in this Set
- Front
- Back
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How many amino acids are incorporated into proteins?
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20
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All amino acids can act as an acid or a base. The term for this ability is what?
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amphoteric
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All amino acids except one that we are concerned with exist in what form?
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L-form
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What single amino acid is not in the L-form and why
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Glycine is not in the L form b/c Glycine does not contain a chiral carbon.
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What is a chiral carbon?
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Means that the carbon has a different compound at each binding site.
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Ten amino acids are considered essential in the adult. What are the 10?
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PVT TIM HALL
P=phenylalanine V=valine T=tryptophan T=threonine I=Isoleucine M=methionine H=histidine A=arginine L=leucine L- lysine |
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In addition to the ten essential amino acids children also need an additional amino acid. What is it?
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Histidine
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Purely ketogenic amino acids are?
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Leucine and lysine
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Lysine is the precursor to what substance?
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carnitine (hicks)
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Carnitine takes fatty acids into the mitochondria for what purpose?
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B-oxidation
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What 3 amino acids are considered aromatic?
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phenylalanine
tyrosine tryptophan |
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How many essential amino acids are also aeromatic?
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2 phenylalnine and tryptophan
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What 3 amino acids are sulfur containing?
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cysteine, methionine, cystine
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What are the 3 branch chained amino acids?
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leucine, isoleucine and valine
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A certain condition exist that causes the px's urine to smell like maple syrup. The basic issue in this condition is the inability to do what?
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Break down branched chain Amino Acids
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What are the 2 acidic amino acids?
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aspartate (aspartic acid)
Glutamate (glutamic acid) |
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What are the 3 basic amino acids?
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(HAL)
histidine arginine lysine note: basic aa have the greatest + net charge at normal blood Ph |
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Wheat and rice both have some amino acids but are not a complete source due to lack of what aa?
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Lysine
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Legumes and pulses have some amino acids but are not a complete source due to lack of what aa?
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Tryptophan and methionine (or cysteine)
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maize has some amino acids but is not a complete source due to lack of what aa?
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Lysine and tryptophan
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Isoelectric point
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ph when an amino acid has no net electric charge (neutral)
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Zwitter ion
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an amino acid at its isoelectric point
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Glutathione
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tripeptide
gylcine + Glutamate + Cysteine |
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Selenium (Se)
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is a mineral for enzyme glutathione peroxidase
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Insulin
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2 polypeptide chains linked by disulfide bonds.
(Insulin does help glucose enter the cell) |
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The characteristic bond of all proteins is the___
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peptide bond
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The peptide bond is a type of_____bond that is specific for protiens.
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amide
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Peptide bond are also known as what?
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C-N bond
Carboxyl-amino bond |
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Peptide bonds are formed by what type of reaction?
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Condensation reaction
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Proteins utilize 4 types of structures what are they?
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Primary
Secondary Tertiary Quaternary |
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Primary protein structures
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Linear sequence
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Secondary protein structures
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alpha-helices and Beta-pleated sheets (both structures are held together by H-bonds between atoms of the polypeptide backbone.
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Tertiary protein structures
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folding of a single polypeptide chain in solution.
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Quaternary protein structures
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association of two or more polypeptide chains to make a functional protien.
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Example of a secondary protein structure
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2 DNA strands together
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Example of a tertiary protein structure
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Myoglobin is the classic example of a globular protein with tertiary structure.
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Example of a quaternary structure
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Hemoglobin
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All enzymes are catalysts. Enzymes increase the rate of reaction by _____.
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lowering the activation energy
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True or false Enzymes are never consumed in reaction.
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True
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The molecule that enzymes act upon is called a______
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substrate
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Km is the measure of what ?
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the affinity that an enzyme has towards the substrate
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Km has an inverse relationship with affinity meaning what?
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lower Km = higher affinity
and higher Km = lower affinity |
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Vmax is equal to what
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Vmax is the max velocity of the enzyme
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Km and Vmax have what relationship?
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Km=1/2 Vmax
(Km: the amount of sustrate required to reach 1/2 Vmax) |
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What are the 3 factors that affect the reaction velocity of an enzyme.
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1. Substrate concentration
2. Temperature 3. Ph |
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Competitive inhibitors
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1. bind to substrate binding site of the enzyme
2. Increase Km (lower affinity) 3. Can add enough substrate to dilute out inhibitors |
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Non-competitive inhibitors
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1. Bind to site other than substrate binding site
2. No change in Km (affinity for biinding site has not changed ) 3. Decreased Vmax (will take longer to reach Vmax) |
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What type of enzyme acts as the rate limiting steps for an entire metabolic pathway?
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Allosteric
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Allosteric enzyme activity is modulated by ______.
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Allosteric effectors
(for example-PFK is allosterically inhibited by an increase of ATP) |
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What is Gibb's free energy?
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Measure of the amount of energy available to determine if a reaction is energetically feasible
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In gibbs free energy if the number is 0 then it is said to be?
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at equilibrium
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In Gibb's free energy a (+) positive number indicates what
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Rxn is non-spontaneous or unfavorable
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In Gibb's free energy a (-) negative number indicates what
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Rxn is spontaneous or favorable
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vitamins are _____ where as minerals are _____
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vit=coenzymes
minerals=cofactors |
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B1 aka as
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Thiamine
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B1 active form
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TPP (thiamine pyrophosphate)
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B1 is used in what type of reaction
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Decarboxylation (loss of CO2)
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B2 aka
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Riboflavin
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B2 active form
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FAD (Falvin-adenine-dinucleotide)
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B2 is involved in what type of reaction?
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Oxidation/reduction via dehydrogenase enzymes
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B3 aka
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niacin
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B3 active forms
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NAD
NADP (nicatinamide adenine dinucleotide) |
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B3 is used in what type of reactions?
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Oxidation/Reductions via dehydrogenase enzymes
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B5 aka
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pantothhenate
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B6 aka
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Pyridoxine
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B6 active form is?
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Pyridoxal-5-phosphate
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B6 is used in what type of reactions?
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1. Transaminations (ketoacid-->Amino acid)
2. amino acid metabolism |
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B7 aka
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Biotin
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B7 active form is?
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Biocytin
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B7 is used in what type of reactions?
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Carboxylation (+co2)
(eg. Acetyl-CoA carboxylase) |
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B9 aka
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Folic acid or folate
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B9 active form is?
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Tetrahydrofolate
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B9 functions in what capacity?
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One carbon transfers (Methyl transfers)
for example DNA and RNA synthesis |
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B12 aka
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Cobalamin
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B12 active form
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Methylcobalamin
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B12 is used in______?
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homocysteine remethylation
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Vitamin C aka
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ascorbic acid
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Vitamin C is used for what ?
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Hydroxylation of proline and lysine in collagen. Enhances iron absorption
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Vitamin A aka
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Retinal
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Most active form of vit A is?
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Retinoic acid
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Vit A is used for?
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vision, growth
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Vitamin D aka
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1,25-Dihydroxy-cholecalciferol
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Vit D is used for ?
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Calcium and phosphate metabolism
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Vit E aka
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alpha-tocopherol
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Vit E function?
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lipid antioxidant
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Vitamin K aka
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Hydroquinone or menadione
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Vitamin K is important in what function?
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Blood clotting, precursor to Coenzyme Q
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Chromium (Cr) function
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Glucose tolerance factor
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Chromium (Cr) metabolism
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helps bind insulin to cell
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Chromium (Cr) deficiency or disease
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Impaired glucose tolerance
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Cobalt(Co) function
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Constituent of vit B12
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Cobalt(Co) deficiency or disease
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pernicious anemia
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Magnesium function
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binds to ATP
Muscle contraction/relaxation protein production many enzymes |
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Magnesium metabolism
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Mg: Ca ratio=1:2
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Magnesium deficiency or disease
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hyperexcitability
muscle weakness sleepiness |
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Iodine (I) function
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Thyroxine T4
Triodothyronine T3 |
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Iodine (I) metabolism
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stored as thyroglobulin
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Iodine (I) deficiency or disease
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Cretinism in children
myxedema in adults |
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Selenium (Se) function
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cofactor, glutathione peroxidase
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Selenium (Se) metabolism
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antioxidant
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Iron (Fe) function
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heme enzyme: hemoglobin, cytochromes
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Iron (Fe) metabolism: it is stored via______ and transported via __________.
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Transported: transferrin
Stored: ferritin |
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Iron (Fe) deficiency
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Hypochromic microcytic anemia
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ZInc (Zn) function
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Cofactor
Carbonic anhydrase |
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Zinc (Zn) metabolism
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Immune system
taste wound healing prostate |
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ZInc (Zn) deficiency
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impaired wound healing
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Flouride (F) function
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increases hardness of teeth
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Flouride (F) deficiency
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dental caries
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In the methylation cycle what enzyme is used?
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Methionine synthase (B12 activates this enzyme)
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In the methylation cycle what does B12 do?
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B12 gives a methyl group to homocysteine
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In the methylation cycle what does B9 do?
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B9 gives methyl group to B12
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A deficiency in B9 will affect what other vitamin?
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B12 and vice versa
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B12 deficiency causes what type of anemia?
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Pernicious, but if the problem is caused by a decrease in intrinsic factor then megablastic anemia (vegetarians)
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Fe3+ is aka
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ferric and is the most active form of iron
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Fe2+ is aka
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ferrous and is most absorbable
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a mineral deficiency in calcium or magnesium results in what condition?
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tetany because calcium and magnesium track together
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What are the antioxidants?
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ACEs
vit A, C, E and Selenium Glutathione, lipoic acid, Co Q 10 |
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PTH has what effect on serum calcium
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It increases serum calcium
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Calcitonin has what affect on serum calcium levels?
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Calcitonin "tones" down calcium in the serum
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Monosaccharides are categorized as what?
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aldehydes or ketones.
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aldehyde group is always found on the ___ carbon
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#1 carbon (C=O or carbonyl is found here)
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Ketone group is always found on the ___ carbon
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#2 carbon (C=O or carbonyl is found here)
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What are the steps to knowing what type of monosaccharide you have?
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1. Count the number of carbons (5=pentose, 6=hexose ect.)
2. Where is the carbonyl (C=O) found (carbon 1 aldo, carbon 2 keto) |
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what type of monosacc is glucose
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aldohexose
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what type of monosacc is galactose
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aldohexose
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what type of monosacc is mannose
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aldohexose
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what type of monosacc is ribose
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aldopentose
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what type of monosacc is fructose
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ketohexose
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Calcitonin has what affect on serum calcium levels?
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Calcitonin "tones" down calcium in the serum
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Monosaccharides are categorized as what?
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aldehydes or ketones.
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aldehyde group is always found on the ___ carbon
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#1 carbon (C=O or carbonyl is found here)
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Ketone group is always found on the ___ carbon
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#2 carbon (C=O or carbonyl is found here)
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What are the steps to knowing what type of monosaccharide you have?
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1. Count the number of carbons (5=pentose, 6=hexose ect.)
2. Where is the carbonyl (C=O) found (carbon 1 aldo, carbon 2 keto) |
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what type of monosacc is glucose
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aldohexose aka dextrose
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what type of monosacc is galactose
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aldohexose
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what type of monosacc is mannose
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aldohexose
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what type of monosacc is ribose
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aldopentose
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what type of monosacc is fructose
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ketohexose aka fruit sugar or levulose
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What is the formula for monosaccharides
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Cn(H2O)n where "n" is the # of carbons.
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An isomer is defined as
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different compounds with the same chemical formula (glucose, fructose, and galactose are all C6H1206)
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An epimer is defined as
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Monosaccharides which differ in their configuration around one specific carbon. Glucose, and Galactose are C-4 epimers. Glucose and mannose are C-2 epimers
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An enantiomer is defined as
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mirror images of the same compound (L- and D- glucose)
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anomer is defined as
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formed when sugars cyclize. Anomers are designated as either alpha or Beta
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If a monosaccharide is represented as a linear stick figure we refer to this as a_____
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Fischer projection
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If a monosaccharide is represented as a Cyclized figure we refer to this as a_____
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haworth projection
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Sucrose linkage
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Glucose+Fructose (a-1,b-2)
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Lactose linkage
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Galactose+Glucose (b-1,4)
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maltose linkage
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glucose+glucose (a-1,4)
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Isomaltose linkage
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glucose+glucose (a-1,6)
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Cellobiose linkage
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glucose+glucose (b-1,4)
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Lactase can break _____
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b-1,4 in lactose
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Amylase breaks
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a-1,4 linkages and forms maltose
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Amylopectin breaks into
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maltose and isomaltose
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Amylose breaks into
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maltose
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glycogen is a polysaccharide found in humans and contains what types or linkages?
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a-1,4 and a-1,6
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amylose and amylopectin are found in plants what are there linkages?
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amylose= a-1,4
Amylopectin= a-1,4 and a-1,6 linkages |
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Cellulose is a polysaccharide found in plants. this polysacc has a linkage that humans cannot break what is it and what do we lack that keeps us from breaking this bond?
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B-1,4 linkage, we lack cellulase
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GAGs or glycosaminoglycans are also called what
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Mucopolysaccharide
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What is a GAG
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a large complex of negatively charged heteropolysaccharides which bind large amounts of water.
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What is the major structural characteristic of GAGs
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a repeating disaccharide unit
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What are the most common GAGS
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Hyaluronic acid found in synovial fluid and chondroitin sulfate in cartilage, tendons and ligaments
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Proteoglycan is defined as what
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a protein core with 1 or more GAGs bound to a H
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What type of bond is characteristic of fats?
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Ester bonds
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Triacylglycerols have three fatty acids esterified to a ________
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gylcerol backbone (an alcohol+an acid) (alcohol+acid=ester bond)
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_____________ are the most predomminant form of fats/lipids in the body and in the diet
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Triacylglycerols
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A fatty acid is composed of what
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a nonpolar hydrocarbon (-CH2-) tail attached to a polar carboxylic acid (COOH) head
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Unsaturated fatty acids contain____bonds
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double
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In unsat fatty acids double bonds do what?
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decrease the melting temperature of fatty acids and raises the freezing point.
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The presence of unsaturated fatty acids in the phospholipid bilayer helps _______________________.
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maintain the fluid nature of the membrane.
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What does hydrogenation of fatty acids do?
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1. to raise the melting point and decrease the freezing point
2. increases shelf life 3.makes a trans fat |
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Oxidation is the ____of a e- or H
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loss
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Reduction is the ___of a e- or H
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gain
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the generation of an unsaturated fat from a saturated fat is what type of reaction?
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Oxidation
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What are the essential fatty acids?
|
linoleic (omega 6- sunflower, safflower, corn oil)
linolenic (omega 3- flax) Arachidonic acid (Omega 6- animal products ) |
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Arachidonic acid is a precursor to what
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prostaglandins
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What are the 3 most saturated oils?
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1. coconut
2. palm kernal 3. Butter |
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for every 2 carbons in a fat = how many acetyl-coa
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1
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what are the important saturated fats and how many carbons do they have?
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Lauric- 12
myristic- 14 palmitic- 16 stearic- 18 |
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what are the important unsaturated fats and how many carbons do they have?
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Oleic acid - 18 (cis is 1 C=C)
linoleic - 18 (cis is 2 C=C) linolenic - 18 (cis is 3 C=C) arachidonic - 20 (cis is 4 C=C) |
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What are the two main classes of nonglycerol lipids
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sphingolipids and steroids
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A deficiency in ___________enzyme is implicated in the degradation of sphingomyelin which results in niemann-pick disease
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sphingomyelinase
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What is the most abundant sterol in humans?
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cholesterol
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Cholesterol is derived from what?
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Acetyl CoA
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What is the rate limiting enzyme in cholesterol synthesis?
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HMG-CoA reductase
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What is the rate limiting step in cholesterol synthesis
|
HMG-CoA ---> mevalonate
using HMG-CoA reductase |
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What is the rate limiting enzyme in steroid biosynthesis
|
desmolase
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what is the rate limiting step in steroid biosynthesis
|
cholesterol ----> pregnenolone
using desmolase |
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Once pregnenolone is produced it is converted into ________ from which all other steroid hormones are derivied.
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progesterone
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What is the rate limiting enzyme of ketone body synthesis?
|
HMG-CoA Synthase
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Chylomicrons are produced and secreted from
|
intestinal mucosal cells
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Chylomicrons are produced in response to what
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Dietary intake of fats (that is, dietary fats are absorbed and repackaged as chylomicrons)
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Chylomicrons carry _____ to peripheral tissues and also carry ____
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triacylglycerides
dietary fats and chlesterol |
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VLDL is synthesized and secreted from the
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liver
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VLDL transports _____ to the peripheral tissues from the liver.
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TAGS
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LDL are derived from
|
VLDL (VlDL-->IDL-->LDL)
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The function of LDL is to transports _________.
|
cholesterol from the liver to tthe peripheral tissues
(LDL= Leaves Da Liver) contains the most cholesterol |
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HDL is synthesized and secreted from the ____
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liver
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The function of HDL is to
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transport cholesterol from the peripheral tissue back to the liver.
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High plasma levels of LDL leads to ____ risk of heart disease, High plasma levels of HDL leads to a ___ risk of heart disease
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increased
decreased |
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True of false As the density of lipoproteins increase TAGs decrease and protein increases
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True
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Put the fats in order from most dense to least dense
|
HDL
LDL IDL VLDL Chylomicrons |
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Put the fats in order from most fat to least fat
|
Chylomicrons
VLDL IDL LDL HDL |
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DNA and RNA are composed of _______, a ________, and a ______ base
|
phosphate, pentose sugar, nitrogenous base.
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The formation of deoxyribose from ribose is what type of reaction?
|
Reduction because you gained a H
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Phosphatase
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removes phosphate
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phosphorylase
|
adds a phosphate
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kinase
|
moves phosphates around
|
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dehydrogenase
|
oxidation/reduction reactions
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carboxylase
|
adds a carbon
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decarboxylase
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removes a carbon
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What is the rate limiting enzyme in glycolysis?
|
PFK
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Aerobic and anaerobic glycolysis nets how many ATP in one pass?
|
2 in 4 out net of 2
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