Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870558 | FEBS Letters | 2014 | 5 Pages |
Abstract
LodA is a novel lysine-ε-oxidase which possesses a cysteine tryptophylquinone cofactor. It is the first tryptophylquinone enzyme known to function as an oxidase. A steady-state kinetic analysis shows that LodA obeys a ping-pong kinetic mechanism with values of kcat of 0.22 ± 0.04 sâ1, Klysine of 3.2 ± 0.5 μM and KO2 of 37.2 ± 6.1 μM. The kcat exhibited a pH optimum at 7.5 while kcat/Klysine peaked at 7.0 and remained constant to pH 8.5. Alternative electron acceptors could not effectively substitute for O2 in the reaction. A mechanism for the reductive half reaction of LodA is proposed that is consistent with the ping-pong kinetics.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Esha Sehanobish, Sooim Shin, Antonio Sanchez-Amat, Victor L. Davidson,