Bacterial Hydrazine Biosynthetic Pathways Featuring Cupin/Methionyl tRNA Synthetase‐like Enzymes

Author:

Matsuda Kenichi1ORCID,Wakimoto Toshiyuki1ORCID

Affiliation:

1. Faculty of Pharmaceutical Sciences Hokkaido University Kita 12, Nishi 6, Kita-ku Sapporo 060-0812 Japan

Abstract

AbstractNitrogen‐Nitrogen (N−N) bond‐containing functional groups in natural products and synthetic drugs play significant roles in exerting biological activities. The mechanisms of N−N bond formation in natural organic molecules have garnered increasing attention over the decades. Recent advances have illuminated various enzymatic and nonenzymatic strategies, and our understanding of natural N−N bond construction is rapidly expanding. A group of didomain proteins with zinc‐binding cupin/methionyl‐tRNA synthetase (MetRS)‐like domains, also known as hydrazine synthetases, generates amino acid‐based hydrazines, which serve as key biosynthetic precursors of diverse N−N bond‐containing functionalities such as hydrazone, diazo, triazene, pyrazole, and pyridazinone groups. In this review, we summarize the current knowledge on hydrazine synthetase mechanisms and the various pathways employing this unique bond‐forming machinery.

Funder

Ministry of Education, Culture, Sports, Science and Technology

Japan Foundation for Applied Enzymology

Japan Agency for Medical Research and Development

Japan Science and Technology Agency

Publisher

Wiley

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