Nitrogen metabolic map of Escherichia coli mediated by multi-functional aminotransferases

Authors

Hataya, S., Ferreira, M., Soleymani, F., Fukui, S., Oliveira, M. d. V. V., Koper, K., Takasuka, T. E., Nikoloski, Z., Maeda, H.

Abstract

Nitrogen is a key element of organic molecules essential to all life. Unlike extensively characterized carbon metabolic maps, it remains elusive how assimilated nitrogen flows through metabolic networks. Here we determined the nitrogen metabolic map of Escherichia coli and used it to construct an enzyme-constrained metabolic model that includes multi-functionality of aminotransferase enzymes responsible for nitrogen transfer reactions. We characterized substrate specificities of sixteen E. coli aminotransferase enzymes by evaluating 2,528 reactions, uncovering 56 previously unrecognized activities. The cellular concentrations of these aminotransferase enzymes were quantified and used to estimate their catalytic rates across all enzyme-substrate pairs, leading to improved predictions of nitrogen flows in E. coli. This work advances our fundamental understanding of the nitrogen metabolic map critical for metabolism and growth.

Preprint server: bioRxiv
The authors list and abstract were imported from bioRxiv on 01 Aug 2026.

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