Properties of Lysine ,3-Aminomutase

Lysine 2,3-aminomutase (LAM) catalyzes the interconversion of L-lysine and L-P-lysine according to Eq. 1  

The enzyme was originally described as a hexamer of identical subunits (47 kDa) that contained iron and pyridoxal S -phosphate (PLP) and was activated by 5-adenosylmethionine (SAM) as well as added iron and PLP. The molecular weight was found to be about 260 kDa. Chemical degradation and cross-linking experiments indicate that the protein is assembled from identical subunits as a trimer of dimers. Thus, two types of intersubunit interactions must exist in the assembled hexamer, those that preferentially contribute to the assembly of dimers, which may be the catalytic units, euid those that allow the association of three dimers into a hexameric unit. 

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