9th SINAPSE Neuro-oncology Imaging Meeting [rescheduled] Mar 11, 2021 09:30 AM - 03:30 PM — West Park Conferencing & Events, 319 Perth Road, Dundee DD2 1NN
Total Body PET 2020 conference [rescheduled] Jun 05, 2021 - Jun 07, 2021 — McEwan Hall, University of Edinburgh
Medical Imaging Convention [rescheduled] Sep 15, 2021 - Sep 16, 2021 — National Exhibition Centre, Birmingham, England


SINAPSE experts from around Scotland have developed ten online modules designed to explain medical imaging. They are freely available and are intended for non-specialists.

Edinburgh Imaging Academy at the University of Edinburgh offers the following online programmes through a virtual learning environment:

Neuroimaging for Research MSc/Dip/Cert

Imaging MSc/Dip/Cert

PET-MR Principles & Applications Cert

Applied Medical Image Analysis Cert

Online Short Courses

The fluorinase, the chlorinase and the duf-62 enzymes

Author(s): H. Deng, D. O'Hagan

The fluorinase from Streptomyces cattleya and chlorinase from Salinispora tropica have a commonality in that they mediate nucleophilic reactions of their respective halide ions to the C-5' carbon of S-adenosyl-L-methionine (SAM). These enzyme reactions fall into the relatively small group of S(N)2 substitution reactions found in enzymology. These enzymes have some homology to a larger class of proteins expressed by the duf-62 gene, of which around 200 representatives have been sequenced and deposited in databases. The duf-62 genes express a protein which mediates a hydrolytic cleavage of SAM to generate adenosine and L-methionine. Superficially this enzyme operates very similarly to the halogenases in that water/hydroxide replaces the halide ion. However structural examination of the duf-62 gene product reveals a very different organisation of the active site suggesting a novel mechanism for water activation.

Full version: Available here

Click the link to go to an external website with the full version of the paper

ISBN: 1367-5931
Publication Year: 2008
Periodical: Current Opinion in Chemical Biology
Periodical Number: 5
Volume: 12
Pages: 582-592
Author Address: