Chapter 15. Cell and Molecular Biology Flashcards
What neurotransmitter does catalization of glutamate decarboxylase produce?
Gamma amino butyric acid (GABA neurotransmitter)
What precursor serves the Epinephrine (after the Phenylalanine) and Thyroxine neurotransmitter?
Catalyzed by this gives phenyl 3-4 quinone than polymerization given Melatonin (black skin pigment)
Tyrosine
*also a.a. precursor of cathecholamine
What precursor serves Serotonin neurotransmitter and Niacin?
Tryptophan
5HT is?
5-hydroxy tryptamine or Serotonin
From precursors Nitric Oxide, Urea and Creatinine serves what amino acid?
Arginine
Also known as fatty acid oxidation.
Ketogenesis
Collectively known as ketone bodies.
betahydroxy butyric acid 80%
acetoacetic acid 20%
acetone trace amounts
Essential amino acids?
PVT TIM HALL
Also known as phosphogluconate pathway and hexose monophosphate shunt. Takes place in where?
Pentose Phosphate Pathway
-Cytosol
Ammonia is converted to what which is nontoxic.
Glutamine (Gln)
During Mitochondrial process, pyruvate to CO2 and H2O is what process?
Oxidative phosphorylation
What type of cycle intermediate forms amino acids such as aspartate and glutamate?
Anabolism
Where does glycolysis occur in most organs of the body?
Cytosol and mitochondria
This cycle takes place in bacterias in place of the Krebs cycle.
Centers on conversion of ACoa to succinate for carb synthesis.
Glyoxylate cycle
The only amino acid without a chiral center. Aa precursor of hemoglobin.
Glycine
Amino acids are precursors of what and from what are those derived from?
Porphyrines, derived from glycine and succinyl-Coa
Several genetic defects in heme biosynthesis.
Uroporphyrinogen III cosynthase deficiency, congenital erythropoietic porphyria.
Red urine, reddish teeth, photosensitive skin, increased hair growth
Ferrochelatase deficiency = erythropoietic porphyria
T or F. There are 10 EAA and humans only require 7 of them.
False. All humans require 8 EAAs.
Infant require histidine.
Define Zwitter ion and Isoelectric point.
Zwitter ion - a molecule or ion having separate positively and negatively charged groups.
pI- pH at which there is no net charge on the structure.
pH>pI negative charge
pH
Define primary, secondary, tertiary and quaternary protein structures.
Primary- linear sequence of aa
Secondary- linked by H bonds
Tertiary- attractions between alpha helices and pleated sheets. 3D struc. formed by disulfide bonds.
Quaternary- more than one aa chain
In tertiary structure: \_\_\_\_\_ interaction between non polar aa \_\_\_\_\_ bonds between polar aa ionic bonds between \_\_\_\_\_ aa \_\_\_\_\_ bonds between Sulfur containing aa
Hydrophobic
Hydrogen
ionic
Covalent
Simple proteins are naturally occuring proteins wc upon hydrolysis yield only what type of aa and give examples.
Alpha aa.
Albumins Globulins Prolamines Glutelin Albuminoids
Examples of Hemoglobinopathies.
Sickle cell anemia, haemoglobin C disease (HbC) and thalassemia syndrome
A cell membrane is composed of what bilayer and its phospholipids are composed of what.
Lipid bilayer
outer portion of membrane- hydrophilic head
inner portion of membrane- hydrophobic chains
Difference between Hemoglobin and Myoglobin.
Hemoglobin- transports O2 I’m blood only. CO2 and CO binds reversibly. Porphyrin ring is a tetramer
Myoglobin- transports O2 in tissues. Present in heart and tissues. -Monomer
end products of: Aerobic glycolysis Anaerobic aa (protein) synthesis purine cycle
pyruvate
lactate
urea
uric acid
Krebs cycle occurs in?
Glycolysis?
Glycosolipid metabolism?
Mitochondria
Cytosol and mitochondria
Cytoplasm
Deficiency in this trace element: Zn Se Cr Mo
Zn- children: poor growth, impaired sex. dev -adults: dermatitis
Se- cardiomyopathy
Cr- impaired glucose tolerance
Mo- present in xanthine oxidase (conversion of purine to uric acid)
