Specific enzymes/processes Flashcards
Aromatic amino acid synthesis (tryptophan, tyrosine and phenylalanine)
DAHP synthase catalyses joining of phosphoenolpyruvate to erythrose-4-phosphate (forming DAHP)
Chorismate intermediate – tryptophan
Later prephenate intermediate - phenylpyruvate — phenylalinine
OR – hydroxyphenylphyruvate – tyrosine
Chorismate and prephenate are inhibited by their respective AA (sequential inhibition)
Purine biosynthesis
Amidophosphoribosyl transferase = catalyses step one, AMP and GMP synergistically inhibit
Aspartokinase - isoenzymes forming threonine, methionine or lysine from aspartate in E. coli
AspI - inhibited by lysine
AspII - by gene expression responding to cellular Met levels (high = repressed, course control)
AspIII - threonine inhibits
Ile - Thr = linear pathway
Thr - Asp = sequential pathway
AspI-III = nested inhibition
Glycogen phosphorylase
Converts glycogen to digestible glucoe-1-phosphate
Dimer with interconvertible forms, active a and inactive b
Phosphorylation of Ser14 residue on each half of the dimer activates, from adrenaline
AMP allosterically activates the enzyme as well
Glutamine synthetase
Done in notes, for transport of nitrogen
Lactic acid dehydrogenase
Isoenzymes in heart, muscle and liver had differing half- lives, involved in carbohydrate processing
Acetyl CoA carboxylase
Lipid synthesis, degraded more rapidly in fasted conditions
HMG-CoA reductase
Cholesterol metabolism, has a bipartite structure with a catalytic cytoplasmic region and a membrane domain to sense degradation signals
Sterols bind the sensing domain.
E3 gp78 binds in the cytosol, and ubiquitinates Lys residues 89 and 248
Blockage of first step of sterol synthesis (in response to high dietary intake??)
Course control – 15-16 hours half life normally, reduced to 2 in this state