Natural history of <Emphasis Type="Italic">S</Emphasis>-adenosylmethionine-binding proteins |
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Authors: | Email author" target="_blank">Piotr?Z?KozbialEmail author Arcady?R?Mushegian |
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Institution: | (1) Stowers Institute for Medical Research, 1000 E. 50th St., Kansas City, MO 64110, USA;(2) Department of Microbiology, Molecular Genetics, and Immunology, University of Kansas Medical Center, Kansas City, Kansas 66160, USA |
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Abstract: | Background
S-adenosylmethionine is a source of diverse chemical groups used in biosynthesis and modification of virtually every class
of biomolecules. The most notable reaction requiring S-adenosylmethionine, transfer of methyl group, is performed by a large class of enzymes, S-adenosylmethionine-dependent methyltransferases, which have been the focus of considerable structure-function studies. Evolutionary
trajectories of these enzymes, and especially of other classes of S-adenosylmethionine-binding proteins, nevertheless, remain poorly understood. We addressed this issue by computational comparison
of sequences and structures of various S-adenosylmethionine-binding proteins. |
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Keywords: | |
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