Kinetic characterization of acetone monooxygenase from Gordonia sp. strain TY-5.

ABSTRACT: Acetone monooxygenase (ACMO) is a unique member of the Baeyer-Villiger monooxygenase (BVMO) family based on its ability to act on small ketones, such as acetone. Herein, we performed a kinetic analysis of ACMO from the propane-utilizing bacterium Gordonia sp. strain TY-5 to assess its preference for smaller ketone substrates. Steady state kinetic analysis of ACMO with a range of linear (C3-C7) and cyclic ketones (C4-C6) reveals that the enzyme elicits the highest catalytic efficiency towards butanone and cyclobutanone. Stopped-flow and inhibition studies further revealed that ACMO has a relatively weak binding affinity for the coenzyme with a dissociation constant of 120 μM. We show through mutagenesis that sequence variation in the residue that coordinates to the 2'-phosphate of NADP(H) p

SUBMITTER: Fordwour OB 

PROVIDER: S-EPMC6215540 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature