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Lysine 2,3-aminomutase (KAM or LAM) (EC |220.127.116.11) is an enzyme which facilitates the conversion of the amino acid Lysine to Beta-Lysine. 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:
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.
Three key cofactors are required for the reaction catalyzed by the Lysine 2,3-aminomutase enzyme. They are:
The generalized reaction takes place in 5 steps:
The reaction mechanism described above is shown below:
 Frey, P.A. "Lysine 2,3-aminomutase: is adenosylmethionine a poor man's adenosylcobalamin. FASEB Jour.; 1993; Vol. 7, 662-670.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Lysine_2,3-aminomutase". A list of authors is available in Wikipedia.|