Benzylmalonyl-CoA dehydrogenase, an enzyme involved in bacterial auxin 
degradation

Schuhle, Karola; Saft, Martin; Voegeli, Bastian; Erb, Tobias J.; Heider, Johann

doi:10.1007/s00203-021-02406-3

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Benzylmalonyl-CoA dehydrogenase, an enzyme involved in bacterial auxin degradation

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Voegeli, Bastian
Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Erb, Tobias J.
Understanding and Building Metabolism, Department of Biochemistry and Synthetic Metabolism, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Center for Synthetic Microbiology (SYNMIKRO), Philipps University of Marburg, Marburg;

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https://doi.org/10.1007/s00203-021-02406-3
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Citation

Schuhle, K., Saft, M., Voegeli, B., Erb, T. J., & Heider, J. (2021). Benzylmalonyl-CoA dehydrogenase, an enzyme involved in bacterial auxin degradation. Archives of Microbiology, 203(7), 4149-4159. doi:10.1007/s00203-021-02406-3.

Cite as: https://hdl.handle.net/21.11116/0000-000A-A76D-0

Abstract

A novel acyl-CoA dehydrogenase involved in degradation of the auxin indoleacetate by Aromatoleum aromaticum was identified as a decarboxylating benzylmalonyl-CoA dehydrogenase (IaaF). It is encoded within the iaa operon coding for enzymes of indoleacetate catabolism. Using enzymatically produced benzylmalonyl-CoA, the reaction was characterized as simultaneous oxidation and decarboxylation of benzylmalonyl-CoA to cinnamoyl-CoA and CO2. Oxygen served as electron acceptor and was reduced to H2O2, whereas electron transfer flavoprotein or artificial dyes serving as electron acceptors for other acyl-CoA dehydrogenases were not used. The enzyme is homotetrameric, contains an FAD cofactor and is enantiospecific in benzylmalonyl-CoA turnover. It shows high catalytic efficiency and strong substrate inhibition with benzylmalonyl-CoA, but otherwise accepts only a few medium-chain alkylmalonyl-CoA compounds as alternative substrates with low activities. Its reactivity of oxidizing 2-carboxyacyl-CoA with simultaneous decarboxylation is unprecedented and indicates a modified reaction mechanism for acyl-CoA dehydrogenases, where elimination of the 2-carboxy group replaces proton abstraction from C2.