Structural and functional characterisation of the methionine adenosyltransferase from Thermococcus kodakarensis.
Schlesier, J., Siegrist, J., Gerhardt, S., Erb, A., Blaesi, S., Richter, M., Einsle, O., Andexer, J.N.(2013) BMC Struct Biol 13: 22-22
- PubMed: 24134203 
- DOI: https://doi.org/10.1186/1472-6807-13-22
- Primary Citation of Related Structures:  
4L4Q - PubMed Abstract: 
Methionine adenosyltransferases catalyse the synthesis of S-adenosylmethionine, a cofactor abundant in all domains of life. In contrast to the enzymes from bacteria and eukarya that show high sequence similarity, methionine adenosyltransferases from archaea diverge on the amino acid sequence level and only few conserved residues are retained.
Organizational Affiliation: 
Institute of Pharmaceutical Sciences, Albert-Ludwigs-University Freiburg, Albertstr, 25, Freiburg D-79104, Germany. jennifer.andexer@pharmazie.uni-freiburg.de.