Ontology highlight
ABSTRACT:
SUBMITTER: Mathevon C
PROVIDER: S-EPMC1948905 | biostudies-literature | 2007 Aug
REPOSITORIES: biostudies-literature
Mathevon Carole C Pierrel Fabien F Oddou Jean-Louis JL Garcia-Serres Ricardo R Blondin Geneviève G Latour Jean-Marc JM Ménage Stéphane S Gambarelli Serge S Fontecave Marc M Atta Mohamed M
Proceedings of the National Academy of Sciences of the United States of America 20070806 33
MiaE catalyzes the posttranscriptional allylic hydroxylation of 2-methylthio-N-6-isopentenyl adenosine in tRNAs. The Salmonella typhimurium enzyme was heterologously expressed in Escherichia coli. The purified enzyme is a monomer with two iron atoms and displays activity in in vitro assays. The type and properties of the iron center were investigated by using a combination of UV-visible absorption, EPR, HYSCORE, and Mössbauer spectroscopies which demonstrated that the MiaE enzyme contains a nonh ...[more]