Overbearingminds Posted January 12, 2011 Posted January 12, 2011 To make a long story short E1 (a protein) reacts with Ubiquitin (another protein) and covalently bonds via a cysteine residue....what type of reaction mechanism are we looking at here? The reaction is ATP dependent if it helps. Thanks a lot in advance.
Horza2002 Posted January 12, 2011 Posted January 12, 2011 The ubiquitin has a carboxylic acid which is activated by ATP with a Mg2+ ion that helps activate the molecule. The activated phosphoester is attacked by the thiol of the E1 enzyme. As far as I can see, thats what you've asked for. http://en.wikipedia.org/wiki/Ubiquitin There is alot of information on this webpage about the mechanisms if you want. ubiq.pdf
Overbearingminds Posted January 12, 2011 Author Posted January 12, 2011 Perfect! Just what I needed to know! Thanks Horza
Horza2002 Posted January 12, 2011 Posted January 12, 2011 No problemo. Im not 100% sure of the mechanism, however thioester bonds are normally formed in this manor (i.e. in polyketide synthase enzymes)
hypervalent_iodine Posted January 15, 2011 Posted January 15, 2011 Checked out your mechanism, Horza. It seems perfectly logical to me!
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