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

Imidazole propionate (ImP) produced by gut microbiota has been associated with type 2 diabetes. Here, the authors present crystal structures of the ImP biosynthesis enzyme urocanate reductase in four different states, providing molecular insights into its catalytic mechanism.

Bibliographic Details
Main Authors: Raminta Venskutonytė, Ara Koh, Olof Stenström, Muhammad Tanweer Khan, Annika Lundqvist, Mikael Akke, Fredrik Bäckhed, Karin Lindkvist-Petersson
Format: Article
Language:English
Published: Nature Publishing Group 2021-03-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-21548-y
id doaj-51b05c6e4427465ea9174681f26b1d76
record_format Article
spelling doaj-51b05c6e4427465ea9174681f26b1d762021-03-11T11:31:37ZengNature Publishing GroupNature Communications2041-17232021-03-0112111110.1038/s41467-021-21548-yStructural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate productionRaminta Venskutonytė0Ara Koh1Olof Stenström2Muhammad Tanweer Khan3Annika Lundqvist4Mikael Akke5Fredrik Bäckhed6Karin Lindkvist-Petersson7Experimental Medical Science, Medical Structural Biology, BMC C13, Lund UniversityDepartment of Molecular and Clinical Medicine/Wallenberg Laboratory, Institute of Medicine, University of GothenburgBiophysical Chemistry, Center for Molecular Protein Science, Department of Chemistry, Lund UniversityDepartment of Molecular and Clinical Medicine/Wallenberg Laboratory, Institute of Medicine, University of GothenburgDepartment of Molecular and Clinical Medicine/Wallenberg Laboratory, Institute of Medicine, University of GothenburgBiophysical Chemistry, Center for Molecular Protein Science, Department of Chemistry, Lund UniversityDepartment of Molecular and Clinical Medicine/Wallenberg Laboratory, Institute of Medicine, University of GothenburgExperimental Medical Science, Medical Structural Biology, BMC C13, Lund UniversityImidazole propionate (ImP) produced by gut microbiota has been associated with type 2 diabetes. Here, the authors present crystal structures of the ImP biosynthesis enzyme urocanate reductase in four different states, providing molecular insights into its catalytic mechanism.https://doi.org/10.1038/s41467-021-21548-y
collection DOAJ
language English
format Article
sources DOAJ
author Raminta Venskutonytė
Ara Koh
Olof Stenström
Muhammad Tanweer Khan
Annika Lundqvist
Mikael Akke
Fredrik Bäckhed
Karin Lindkvist-Petersson
spellingShingle Raminta Venskutonytė
Ara Koh
Olof Stenström
Muhammad Tanweer Khan
Annika Lundqvist
Mikael Akke
Fredrik Bäckhed
Karin Lindkvist-Petersson
Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production
Nature Communications
author_facet Raminta Venskutonytė
Ara Koh
Olof Stenström
Muhammad Tanweer Khan
Annika Lundqvist
Mikael Akke
Fredrik Bäckhed
Karin Lindkvist-Petersson
author_sort Raminta Venskutonytė
title Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production
title_short Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production
title_full Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production
title_fullStr Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production
title_full_unstemmed Structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production
title_sort structural characterization of the microbial enzyme urocanate reductase mediating imidazole propionate production
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-03-01
description Imidazole propionate (ImP) produced by gut microbiota has been associated with type 2 diabetes. Here, the authors present crystal structures of the ImP biosynthesis enzyme urocanate reductase in four different states, providing molecular insights into its catalytic mechanism.
url https://doi.org/10.1038/s41467-021-21548-y
work_keys_str_mv AT ramintavenskutonyte structuralcharacterizationofthemicrobialenzymeurocanatereductasemediatingimidazolepropionateproduction
AT arakoh structuralcharacterizationofthemicrobialenzymeurocanatereductasemediatingimidazolepropionateproduction
AT olofstenstrom structuralcharacterizationofthemicrobialenzymeurocanatereductasemediatingimidazolepropionateproduction
AT muhammadtanweerkhan structuralcharacterizationofthemicrobialenzymeurocanatereductasemediatingimidazolepropionateproduction
AT annikalundqvist structuralcharacterizationofthemicrobialenzymeurocanatereductasemediatingimidazolepropionateproduction
AT mikaelakke structuralcharacterizationofthemicrobialenzymeurocanatereductasemediatingimidazolepropionateproduction
AT fredrikbackhed structuralcharacterizationofthemicrobialenzymeurocanatereductasemediatingimidazolepropionateproduction
AT karinlindkvistpetersson structuralcharacterizationofthemicrobialenzymeurocanatereductasemediatingimidazolepropionateproduction
_version_ 1724225488634773504