Two Different Quinohemoprotein Amine Dehydrogenases Initiate Anaerobic Degradation of Aromatic Amines in Aromatoleum aromaticum EbN1

Author:

Schmitt Georg1,Saft Martin1,Arndt Fabian1,Kahnt Jörg2,Heider Johann13

Affiliation:

1. Laboratory for Microbial Biochemistry, Philipps University of Marburg, Marburg, Germany

2. Max Planck Institute for Terrestrial Microbiology, Marburg, Germany

3. LOEWE-Center for Synthetic Microbiology, Marburg, Germany

Abstract

The known substrate spectrum of A. aromaticum EbN1 is expanded toward aromatic amines, which are metabolized as sole substrates coupled to denitrification. The characterization of the two quinohemoprotein isoenzymes involved in degrading either 2-PEA or BAm expands the knowledge of this enzyme family and establishes for the first time that the necessary maturation of their quinoid CTQ cofactors does not require the presence of molecular oxygen. Moreover, the study revealed a highly interesting regulatory phenomenon, suggesting that growth with BAm leads to a complete replacement of 2-PEADH by BAmDH, which has considerably different catalytic and inhibition properties.

Funder

DFG

Synmikro Center

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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