ArticleAMB Express2018
Kinetic characterization of acetone monooxygenase from Gordonia sp. strain TY-5.
Article in AMB Express, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 16 citations in OpenAlex.
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- Complete Genome Sequence and Function Gene Identify of Prometryne-Degrading StrainMicroorganisms · 2021Article
- Structure-Based Redesign of a Self-Sufficient Flavin-Containing Monooxygenase towards Indigo Production.International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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) partially accounts for the weaker binding affinity observed. As for shown for related BVMOs, NADP
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