Lysine 2,3-aminomutase

Lysine 2,3-aminomutase (KAM or LAM) (EC 5.4.3.2) is a radical SAM enzyme that facilitates the conversion of the amino acid lysine to beta-lysine.

[1] 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.

[2] KAM was first purified and characterized in Clostridium subterminale for studies of Lysine metabolism.

Four key cofactors are required for the reaction catalyzed by the lysine 2,3-aminomutase enzyme.

Reaction catalyzed by KAM
Pyridoxal phosphate