L5 - PTM Flashcards
What is PTM?
addition of a chemical group or molecule to specific amino acids of a protein
What do PTMs do?
provide a means to control protein activity, function, stability, interactions or localisation
What do we use to add/remove groups to proteins?
enzymes
PTMs can
- create/block binding sites
- change confirmation of a protein
- affect the stability of a protein
- rapid signal amplificatio
- allow cross-talk
How many protein kinases are there?
538
What molecule is phosphate added from?
ATP
What group of phosphate from ATP is it added from?
gamma
What residues are phosphates added to?
Threonine, tyrosine, serine.
What does protein phosphorylation mediate?
cell signalling
What are the advantages of using phosphorylation & de-P as a control mechanism?
rapid, easily reversible and does not need new proteins to be made/degraded
What sort of charge does phosphorylation add?
Negative
What sort of mechanism occurs in phosphorylation?
Nucleophilic attack
What occurs in the nucleophilic attack in phosphorylation?
- kinase attacks H in OH group in serine, negative O attacks PO3 in ATP = phosphoserine & ADP
What happens in lysine acetylation - charge wise?
Addition of acetyl = neutralising lysine positive charge
What happens if lysine is acetylated?
creates a binding site for specific proteins that recognised acetlylated lysine
What sort of mechanism occurs in lysine acetylation?
Nucleophilic attack
What occurs in the nucleophilic attack in lysine acetylation?
aceytlase attacks the H in NH3, and then N attacks the carbonyl C in acetyl-CoA, then the CoA is removed
How do we make lysine more reactive, activating it for a direct nucleophilic attack on acetyl-CoA
glutmate residue in enzyme activates a H2O molecule, removing a protin from the lysine amine group. deproton = more reactive
What was lysie modification initially characterised as?
histone modifications controlling chromatin structure
