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- W4387472175 abstract "Monoamine oxidases (MAOs) are pivotal regulators of neurotransmitters in mammals, while microbial MAOs have been shown to be valuable biocatalysts for enantioselective synthesis of pharmaceutical compounds or precursors thereof. For extending the knowledge on how MAOs function at molecular level and in order to provide more biocatalytic tools, we set out to identify and study a robust bacterial variant: a MAO from the thermophile Thermoanaerobacterales bacterium (MAOTb ). MAOTb is highly thermostable with melting temperatures above 73 0 C and is well expressed in Escherichia coli. Substrate screening revealed that the oxidase is most efficient with n-alkylamines with n-heptylamine being the best substrate. Pre-steady state kinetic analysis shows that reduced MAOTb rapidly reacts with molecular oxygen confirming that it is a bona fide oxidase. The crystal structure of MAOTb was resolved at 1.5 Å and showed an exceptionally high similarity with the two human monoamine oxidases, MAO A and MAO B. The active site of MAOTb resembles mostly the architecture of human MAO A, including the cysteinyl protein-FAD linkage. Yet, the bacterial MAO lacks a C-terminal extension found in human MAOs, which explains why it is expressed and purified as soluble protein, while the mammalian counterparts are anchored to the membrane through an α-helix. MAOTb also displays a slightly different active site access tunnel, which may explain the specificity towards long aliphatic amines. Being an easy to express, thermostable enzyme, for which a high-resolution structure was elucidated, this bacterial MAO may develop into a valuable biocatalyst for synthetic chemistry or biosensing." @default.
- W4387472175 created "2023-10-11" @default.
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- W4387472175 date "2023-10-09" @default.
- W4387472175 modified "2023-10-12" @default.
- W4387472175 title "Discovery and structural characterization of a thermostable bacterial monoamine oxidase" @default.
- W4387472175 doi "https://doi.org/10.1111/febs.16973" @default.
- W4387472175 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37814408" @default.
- W4387472175 hasPublicationYear "2023" @default.
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