Steady-state kinetic mechanism of LodA, a novel cysteine tryptophylquinone-dependent oxidase
作者： Esha Sehanobish , Sooim Shin , Antonio Sanchez-Amat , Victor L. Davidson
DOI: 10.1016/J.FEBSLET.2014.01.021
关键词:
摘要: LodA is a novel lysine-e-oxidase which possesses cysteine tryptophylquinone cofactor. It the first enzyme known to function as an oxidase. A steady-state kinetic analysis shows that obeys ping-pong mechanism with values of kcat 0.22±0.04 s(-1), Klysine 3.2±0.5 μM and KO2 37.2±6.1 μM. The exhibited pH optimum at 7.5 while kcat/Klysine peaked 7.0 remained constant 8.5. Alternative electron acceptors could not effectively substitute for O2 in reaction. reductive half reaction proposed consistent kinetics.
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