Metabolism Flashcards
What constitutes a protein
An organic compound of a series of 1 or more amino acids, which are essential to life
State all the hydrophobic amino acids
Glycine, Alanine, Proline, Valine, Leucine, Isoleucine, Methionine, Tryptophan, Phenylalanine
State all the hydrophilic amino acids
Glutamine, Cysteine, Asparagine, Tyrosine, Threonine, Serine
State amino acids with charged side chains
Lysine, Arginine, Histidine, Aspartate, Glutamate
Which are protonated at a physiological pH
Lysine, Arginine
Common property between Glutamine and Asparagine
Both negatively charged at physiological pH
What is chiraliy
When 4 different constituents are binded to a carbon atom, giving optical isomerism, and non superimposable molecules
Which protein is always found in the body
The L form
Which is the only non-chiral amino acid
Glycine
Characteristics of a peptide bond
Condensation reaction,
Formed between Carbon and Nitrogen
Kinetically stable
No free rotation around the bond
What bonds hold proteins together
Covalent Hydrogen Ionic Van der Waals Hydrophobic interactions
What is a disulfide bridge
Bond formed between two cysteine side chains that have been oxidised, linking two amino acids
Why is proline considered a ‘kinky’ amino acid
When joined as a side chain, it loses its N-H group, interrupting the hydrogen bonds in the helix, so not symmetrical, so creates a kink
Two common denaturants that are used in labs
Urea
Breaks Hydrogen bonds
2-Mercaptoethonal
breaks disulphide bonds
What are the benefits of a coupled reaction
If an unfavourable reaction ( most synthesis) is coupled with a favourable reaction, and the change in G remains negative, then it can take place
Where is lysosome found
tears and snot
How does it provide defense against bacteria
Catalyses the hydrolysis of a sugar in the cell wall, when the bond breaks, the bacteria dies
State the two essential residues in lysosome
Glu35, Asp52
What is the optimum pH of lysosome
5,5, because Glu35 is unionised, Asp52 is ionised
What type of reaction is NAD+ normally used in
co-factor in dehydrogenation reactions
describe the actions of NAD+ in lactate dehydrogenase
given off when pyruvate ==> lactate
Goes through blood stream to liver with lactate and reconverted into pyruvate
What are the products of glycolysis
2 ATP
2 Pyruvate
What are the products of the TPA or Krebs cycle
3 NADH
1 GTP
1 FADH2
2 CO2
Which Glycolysis steps use ATP
Glucose =hexokinase=> Glucose-6-phosphate
Fructose-6-phosphate =phosphofructokinase=> Fructose-1,6-biphosphate
Which Glycolysis steps produce ATP
1,3- biphosphoglycerate=phosphoglycerate kinase=> 3-phosphoglycerate
phosphoenolpyruvate=pyruvate kinase=> pyruvate
What is the first step in glycolysis
Glucose = hexokinase => Glucose-6-phosphate
What is the second step in glycolysis
Glucose-6-phosphate=>phosphoglucose isomerase=> fructose-6-phosphate
What is the third step in glycolysis
Fructose-6-phosphate= phosphofructokinase=> Fructose-1,6-biphosphate
What is the fourth step in glycolysis
Fructose-1,6-phosphate= adolase =>Glyceraldehyde-3-phosphate + dehydroxyacetone phosphate
What is the fifth step in glycolysis
Dehydroxyacetone phosphate = triose phosphate isomerase=> Glyceraldehyde-3-phosphate
What is the sixth step in glycolysis
Glyceraldehyde-3-phosphate= glyceraldehyde-3-phosphate dehydrogenase=> 1,3-biphosphoglycerate
What is the seventh step in glycolysis
1,3-biphosphoglycerate = phosphoglycerate kinase=> 3-phosphoglycerate
What is the eighth step in glycolysis
3-phosphoglycerate= phosphoglycerate mutase=> 2-phosphoglycerate
What is the ninth step in glycolysis
2-phosphoglycerate=enolase=> phosphoenolpyruvate
What is the tenth step in glycolysis
phosphoenolpyruvate= pyruvate kinase=>pyruvate
What are the three fates of pyruvate
Lactate
Acetyl CoA
Alcohol
