Enzymes 2

Cards (29)

  • What is a transition state analogues?

    compound that inhibit enzyme, largely competetive
  • what binds with a higher affinity TSA or substrate?
    TSA
  • what is a transition state analogues example?

    yeast aldolase, in glycolysis
  • what is Km?
    michaelis constant
  • what does low km a mean?
    high affinity with active site and molecule
  • what is ki?

    same as km for inhibitor
  • how to tell how much stronger is the TSA than natural transition state?
    Km / Ki
  • what is the first step in catalysis?
    formation of enzyme-substrate complex
  • who comes up with the induced-fit hypothesis?
    Koshland
  • where do the catalytic amino acids in the active site come from?

    different locations in the primary amino acid sequences
  • how does the substrates bind in the active site of enzyme?
    multiple weak interactions
  • What type of bond does not form with enzyme and substrate?
    covalent
  • what is the difference between active site and catalytic site?
    Active site: where substrate binds and reactions occur. Catalytic site: where catalysis takes place within the active site.
  • what makes up active site?
    ATP binding-site, substrate binding site, catalytic residues (catalytic site)
  • how does the active site facilitate reactions?
    Entropy effect
    Orbital steering
  • what is the entropy effect?
    Substrates held next to each other or catalytic groups for increased length of time
  • what is orbital steering?
    best orientation of substrate relative to catalytic groups
  • what is induced fit?

    Maximal binding involves changes to conformation of E and S
  • why do enzymes react with any molecule?

    Induced-fit
  • how does induced fit improve specifity?

    open conformation allows substrate binding.
    closed conformation reconstitutes catalytic site
  • what are coenzymes?
    Non-protein organic that binds at catalytic site, normally reversible bound, few permanent prosthetic groups
  • What is an inactive enzyme known as?
    apoenzyme
  • what is an active enzyme called?
    holoenzyme
  • What is a cofactor?
    inorganic mostly metals , that bind NOT at the catalytic site, bind near on in active site
  • what do cofactors do?
    • assist in substrate binding
    • stabilisation of transititon state
    • orientation
    • stabilises the catalytic site
    • Can participate general acid-base catalysis and oxidation-reduction
  • what are the 3 reaction mecahnisms?
    acid-base catalysis, covalent catalysis, electrostatic catalysis
  • what is covalent catalysis?
    covalent link is formed between substrate and amino acid in catalytic site
  • which amino acid is in acid-base catalysis?
    Histidine
  • what is electrostatic catalysis?
    favours formation of transition state by stabilizing its structure