enz 2

• face flushing + tachycardia when small amounts are consumed. symptoms caused by acetylaldehyde CH3CHO • from a Km mutation • aldehyde dehydrogenase clears out the symps. Two types of it cytoplasmic (high Km) and mitochondrial (low Km). • in ppl with the disease, mitoch. enz is less active due to a SINGLE AMINO ACID MUTATION • uncompetitive inhibitor used

plot 1/[S] vs 1/V (y,x) 1/V = (Km / Vmx) * (1/[S]) + 1/Vmax slope = Km/Vmax

Involves control by the amount of product fromed reducing the activity of enzs in the pathways. Accomplished by allosteric regulation

• usually unidirectional enz. • controls a committed / rate limiting step of pathways. • Regulated by a product in the pathway • have a regulatory binding site • modifies Vmax

inhibitor at binding site – Blocks substrate from binding. Increases Km as it decreases binding reversible

allosteric Inhibition at distal/allosteric site. Affects only Vmax by decreasing it

Inhibition at binding site (requires substrate to be present) Aids the binding activity as subs must be present. Decreases Km AND Vmax because catalysis doesnt happen

inhibition at binding site (requires reaction) binds to enz, undergoes catalysis and shuts down the enz. No Vmax or Km. Cell remakes enz slower than transition enz as catalysis happens

Inhibition at binding site inhibitor mimics subs on TS and enzs are shut down due to the high amount of energy it requires to keep inhibitor on TS. Cell degrates enz but inhibitor keeps destroying other enzs. No Km or Vmax Fast when it happens.

is the most common modification used to affect protein function. dramatically changes its charge statues + activity due to high/dif electron

kinase enz catalyzes addition of PO4 to serine/threonine/tyrosine Phosphatase enz removes PO4 from target (moiety)