Talk:Aminoacyl tRNA synthetase
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editthis article has no sources...granted, most of the info here can be found in a biochemistry textbook, what is wikipedia's policy on this?
Is the info on the classes of enzynes correct
editA ppt lecture slide I have states that the class I is a two step mechanism. Step 1: transfer of aminoacyl group to 2' OH. Step 2: aminoacyl group is transfered from 2' to 3'. Also it states that the class II enzymes have a one step mechanism. Further it states that there is only one aminoacyl tRNA synthatase per tRNA. I will look into this when I have more time if someone else doesn't tackle it first. --Drewlew 16:50, 18 August 2007 (UTC)
- Both assumptions are incorrect. The mechanisms you are referring to are both a part of formation of the enzyme-bound aminoacyl-adenylate (step 1) and have nothing to do with transfer to tRNA (step 2). The assumption that there is one aaRS per tRNA is also the classic E. coli paradigm and is not valid for most organisms. Antorjal 03:16, 22 August 2007 (UTC)
An example structure of amino acid ATP → aminoacyl-AMP PPi
editWhat exactly does this look like? — Preceding unsigned comment added by 50.104.217.8 (talk) 06:00, 6 December 2014 (UTC)
Name of the Enzyme
editThe article says:
"Aminoacyl-tRNA-Synthetase"
I have however also read:
"tRNA-Aminoacyl-Synthetase"
Is there some way or reference which one is the correct form? Some convention that visitors could read, in order to find out? 194.166.102.124 (talk) 15:13, 11 August 2012 (UTC)
table by class
editWe could use a table showing which residues are assembled by which class, as in these lecture notes. -- stillnotelf is invisible 18:09, 28 January 2015 (UTC)