Heme-based dioxygenases: Structure, function and dynamics.

Autor: Geeraerts Z; Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, United States., Ishigami I; Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, United States., Gao Y; Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, United States., Yeh SR; Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, United States. Electronic address: syun-ru.yeh@einsteinmed.edu.
Jazyk: angličtina
Zdroj: Journal of inorganic biochemistry [J Inorg Biochem] 2024 Dec; Vol. 261, pp. 112707. Date of Electronic Publication: 2024 Aug 30.
DOI: 10.1016/j.jinorgbio.2024.112707
Abstrakt: Tryptophan dioxygenase (TDO) and indoleamine 2,3 dioxygenase (IDO) belong to a unique class of heme-based enzymes that insert dioxygen into the essential amino acid, L-tryptophan (Trp), to generate N-formylkynurenine (NFK), a critical metabolite in the kynurenine pathway. Recently, the two dioxygenases were recognized as pivotal cancer immunotherapeutic drug targets, which triggered a great deal of drug discovery targeting them. The advancement of the field is however hampered by the poor understanding of the structural properties of the two enzymes and the mechanisms by which the structures dictate their functions. In this review, we summarize recent findings centered on the structure, function, and dynamics of the human isoforms of the two enzymes.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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