Figure 1.
Fig. 1. Aminomutases in the bacterial lysine fermentation
pathway. (A) 5,6-LAM and 2,3-LAM catalyze similar reactions and
act on similar substrates. Both enzymes require PLP, but 5,6-LAM
is AdoCbl-dependent, whereas 2,3-LAM is an AdoMet-dependent
iron-sulfur enzyme. The natural substrates of 5,6-LAM include
DL-lysine and -L-lysine. 2,3-LAM acts
on L-lysine and does not accept D-lysine as a substrate. (B)
Proposed mechanism of 5,6-LAM, modified from ref. 38. The boxed
step represents the state of the enzyme observed in this study.
The unboxed steps are proposed to occur while 5,6-LAM is in the
hypothetical top-on conformation (see the Introduction).
-L-lysine. 2,3-LAM acts
on L-lysine and does not accept D-lysine as a substrate. (B)
Proposed mechanism of 5,6-LAM, modified from ref. 38. The boxed
step represents the state of the enzyme observed in this study.
The unboxed steps are proposed to occur while 5,6-LAM is in the
hypothetical top-on conformation (see the Introduction).