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Article

Full-length in meso structure and mechanism of rat kynurenine 3-monooxygenase inhibition.

Communications biology - 4 Feb 2021

Mimasu Shinya, Yamagishi Hiroaki, Kubo Satoshi, Kiyohara Mie, Matsuda Toshihiro, Yahata Toshiko, Thomson Heather A, Hupp Christopher D, Liu Julie, Okuda Takao, Kakefuda Kenichi

Abstract excerpt

The structural mechanisms of single-pass transmembrane enzymes remain elusive. Kynurenine 3-monooxygenase (KMO) is a mitochondrial protein involved in the eukaryotic tryptophan catabolic pathway and is linked to various diseases. Here, we report the mammalian full-length structure of KMO in its membrane-embedded form, complexed with compound 3 (identified internally) and compound 4 (identified via DNA-encoded...

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PMID: 33542467
DOI: 10.1038/s42003-021-01666-5
PMCID: PMC7862291

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