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Lysine 2,3-aminomutase : ウィキペディア英語版 | Lysine 2,3-aminomutase
Lysine 2,3-aminomutase (KAM or LAM) () is a radical SAM enzyme that facilitates the conversion of the amino acid lysine to beta-lysine.〔Frey, P.A. "Lysine 2,3-aminomutase: is adenosylmethionine a poor man's adenosylcobalamin. ''FASEB Jour.''; 1993; ''Vol. 7'', 662-670.〕〔Lepore, B.; Ruzicka, F.J.; Frey, P.A.; Ringe, D. "The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale. ''PNAS''; 2005; ''102'', 13819-13824.〕 It accomplishes this interconversion using three cofactors and a 5'-deoxyadenosyl radical formed in a S-Adenosyl methionine (SAM) activated radical reaction pathway.() The generalized reaction is shown below:
== Structure ==
Shown on the right is the three-dimensional structure of the Lysine 2,3-aminomutase protein. The structure was determined by X-ray crystallography to 2.1 Angstrom resolution and was seen to crystallize as a homotetramer.() KAM was first purified and characterized in ''Clostridium subterminale'' for studies of Lysine metabolism.
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