Response to Mark Aspin query:

All internal approval has been acquired.  

In actuality, the active site is similar to the enzymes in the other families (this is quite noticeable in Fig 4 where the active sites of examples of the other enzymes are shown). What this means is that if someone wanted to they could probably model the archaeal G1P after one of the many already-published enzymes. However, they would likely run into the same problem as us, with the zinc metal in the active site which makes it extremely difficult to use the structure for in silico screening (a problem we ran into with ComA in previous in silico trials). We think a better strategy is to use the RCC enzyme we already have, and screen the additional 10,000 compounds. We have results already for 5000 compounds and we will identify those in the next report (while still aiming to get the structure for RCC G1P to see if it is any different). So the data in this paper is not strategically critical to targeting this enzyme. Again itâ??s a hyperthermophile and we suspect there to be some functional and distinct differences between it and identical enzymes from the rumen, some of which are definitely centred around the active site. We wouldnâ??t use this particular enzyme in a straight up in silico run, the identity does dip a lot.

Also, I forgot to mention in the that email with the long list of reasons why we thought it would be OK to publish, is that you will have noticed that three other archaeal G1PDHs have been biochemically characterised already, so our biochemical data is not new either. The MJ G1PDH structure will help us with the RCC structure, but not that much, as we used the publically-available bacterial GDH to determine the MJ G1PDH structure, so could do the same for the RCC (when we get the data).
