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DOI	10.1073/pnas.2106561118
	A new regime of heme-dependent aromatic oxygenase superfamily
	Shin I.; Wang Y.; Liu A.
发表日期	2021
ISSN	0027-8424
卷号	118 期号:43
英文摘要	Two histidine-ligated heme-dependent monooxygenase proteins, TyrH and SfmD, have recently been found to resemble enzymes from the dioxygenase superfamily currently named after tryptophan 2,3-dioxygenase (TDO), that is, the TDO superfamily. These latest findings prompted us to revisit the structure and function of the superfamily. The enzymes in this superfamily share a similar core architecture and a histidine-ligated heme. Their primary functions are to promote O-atom transfer to an aromatic metabolite. TDO and indoleamine 2,3-dioxygenase (IDO), the foundingmembers, promote dioxygenation through a two-step monooxygenation pathway. However, the new members of the superfamily, including PrnB, SfmD, TyrH, and MarE, expand its boundaries and mediate monooxygenation on a broader set of aromatic substrates. We found that the enlarged superfamily contains eight clades of proteins. Overall, this protein group is a more sizeable, structure-based, histidine-ligated heme-dependent, and functionally diverse superfamily for aromatics oxidation. The concept of TDO superfamily or heme-dependent dioxygenase superfamily is no longer appropriate for defining this growing superfamily. Hence, there is a pressing need to redefine it as a hemedependent aromatic oxygenase (HDAO) superfamily. The revised concept puts HDAO in the context of thiol-ligated heme-based enzymes alongside cytochrome P450 and peroxygenase. It will update what we understand about the choice of heme axial ligand. Hemoproteins may not be as stringent about the type of axial ligand for oxygenation, although thiolate-ligated hemes (P450s and peroxygenases) more frequently catalyze oxygenation reactions. Histidine-ligated hemes found in HDAO enzymes can likewise mediate oxygenation when confronted with a proper substrate. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Axial ligand; Dioxygenase; Heme; Hydroxylase; Superfamily
语种	英语
scopus关键词	aromatic compound; cytochrome P450; heme oxygenase; hemoprotein; histidine; peroxygenase; SfmD protein; thiol; tryptophan 2,3 dioxygenase; TyrH protein; unclassified drug; chemical structure; controlled study; molecular size; oxidation; oxygenation; protein function; protein structure; Review; structure analysis
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/238324
作者单位	Department of Chemistry, The University of Texas at San Antonio, San Antonio, TX 78249, United States
推荐引用方式 GB/T 7714	Shin I.,Wang Y.,Liu A.. A new regime of heme-dependent aromatic oxygenase superfamily[J],2021,118(43).
APA	Shin I.,Wang Y.,&Liu A..(2021).A new regime of heme-dependent aromatic oxygenase superfamily.Proceedings of the National Academy of Sciences of the United States of America,118(43).
MLA	Shin I.,et al."A new regime of heme-dependent aromatic oxygenase superfamily".Proceedings of the National Academy of Sciences of the United States of America 118.43(2021).