Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production. / Venskutonytė, Raminta; Koh, Ara; Stenström, Olof; Khan, Muhammad Tanweer; Lundqvist, Annika; Akke, Mikael; Bäckhed, Fredrik; Lindkvist-Petersson, Karin.

In: Nature Communications, Vol. 12, No. 1, 2021.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Venskutonytė, R, Koh, A, Stenström, O, Khan, MT, Lundqvist, A, Akke, M, Bäckhed, F & Lindkvist-Petersson, K 2021, 'Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production', Nature Communications, vol. 12, no. 1. https://doi.org/10.1038/s41467-021-21548-y

APA

Venskutonytė, R., Koh, A., Stenström, O., Khan, M. T., Lundqvist, A., Akke, M., Bäckhed, F., & Lindkvist-Petersson, K. (2021). Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production. Nature Communications, 12(1). https://doi.org/10.1038/s41467-021-21548-y

Vancouver

Venskutonytė R, Koh A, Stenström O, Khan MT, Lundqvist A, Akke M et al. Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production. Nature Communications. 2021;12(1). https://doi.org/10.1038/s41467-021-21548-y

Author

Venskutonytė, Raminta ; Koh, Ara ; Stenström, Olof ; Khan, Muhammad Tanweer ; Lundqvist, Annika ; Akke, Mikael ; Bäckhed, Fredrik ; Lindkvist-Petersson, Karin. / Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production. In: Nature Communications. 2021 ; Vol. 12, No. 1.

Bibtex

@article{9718aaa7f2344d269e39b573fdf12b64,
title = "Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production",
abstract = "The human microbiome can produce metabolites that modulate insulin signaling. Type 2 diabetes patients have increased circulating concentrations of the microbially produced histidine metabolite, imidazole propionate (ImP) and administration of ImP in mice resulted in impaired glucose tolerance. Interestingly, the fecal microbiota of the patients had increased capacity to produce ImP, which is mediated by the bacterial enzyme urocanate reductase (UrdA). Here, we describe the X-ray structures of the ligand-binding domains of UrdA in four different states, representing the structural transitions along the catalytic reaction pathway of this unexplored enzyme linked to disease in humans. The structures in combination with functional data provide key insights into the mechanism of action of UrdA that open new possibilities for drug development strategies targeting type 2 diabetes.",
author = "Raminta Venskutonytė and Ara Koh and Olof Stenstr{\"o}m and Khan, {Muhammad Tanweer} and Annika Lundqvist and Mikael Akke and Fredrik B{\"a}ckhed and Karin Lindkvist-Petersson",
year = "2021",
doi = "10.1038/s41467-021-21548-y",
language = "English",
volume = "12",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",
number = "1",

}

RIS

TY - JOUR

T1 - Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production

AU - Venskutonytė, Raminta

AU - Koh, Ara

AU - Stenström, Olof

AU - Khan, Muhammad Tanweer

AU - Lundqvist, Annika

AU - Akke, Mikael

AU - Bäckhed, Fredrik

AU - Lindkvist-Petersson, Karin

PY - 2021

Y1 - 2021

N2 - The human microbiome can produce metabolites that modulate insulin signaling. Type 2 diabetes patients have increased circulating concentrations of the microbially produced histidine metabolite, imidazole propionate (ImP) and administration of ImP in mice resulted in impaired glucose tolerance. Interestingly, the fecal microbiota of the patients had increased capacity to produce ImP, which is mediated by the bacterial enzyme urocanate reductase (UrdA). Here, we describe the X-ray structures of the ligand-binding domains of UrdA in four different states, representing the structural transitions along the catalytic reaction pathway of this unexplored enzyme linked to disease in humans. The structures in combination with functional data provide key insights into the mechanism of action of UrdA that open new possibilities for drug development strategies targeting type 2 diabetes.

AB - The human microbiome can produce metabolites that modulate insulin signaling. Type 2 diabetes patients have increased circulating concentrations of the microbially produced histidine metabolite, imidazole propionate (ImP) and administration of ImP in mice resulted in impaired glucose tolerance. Interestingly, the fecal microbiota of the patients had increased capacity to produce ImP, which is mediated by the bacterial enzyme urocanate reductase (UrdA). Here, we describe the X-ray structures of the ligand-binding domains of UrdA in four different states, representing the structural transitions along the catalytic reaction pathway of this unexplored enzyme linked to disease in humans. The structures in combination with functional data provide key insights into the mechanism of action of UrdA that open new possibilities for drug development strategies targeting type 2 diabetes.

U2 - 10.1038/s41467-021-21548-y

DO - 10.1038/s41467-021-21548-y

M3 - Journal article

C2 - 33649331

AN - SCOPUS:85102223471

VL - 12

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

IS - 1

ER -

ID: 259937686