Allomorphy as a mechanism of post-translational control of enzyme activity

β-phosphoglucomutase (βPGM) from Lactococcus lactis is a phosphoryl transfer enzyme required for catabolism of trehalose and maltose. Coupled analyses of multiple βPGM structures and enzymatic activity lead to the proposal of allomorphy — a post-translational mechanism controlling enzyme activity....

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Main Authors:	Henry P. Wood, F. Aaron Cruz-Navarrete, Nicola J. Baxter, Clare R. Trevitt, Angus J. Robertson, Samuel R. Dix, Andrea M. Hounslow, Matthew J. Cliff, Jonathan P. Waltho
Format:	Article
Language:	English
Published:	Nature Publishing Group 2020-11-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-020-19215-9

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spelling	doaj-b567dab9609e4747a1dcd185585f388f2021-05-11T08:28:55ZengNature Publishing GroupNature Communications2041-17232020-11-0111111210.1038/s41467-020-19215-9Allomorphy as a mechanism of post-translational control of enzyme activityHenry P. Wood0F. Aaron Cruz-Navarrete1Nicola J. Baxter2Clare R. Trevitt3Angus J. Robertson4Samuel R. Dix5Andrea M. Hounslow6Matthew J. Cliff7Jonathan P. Waltho8Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of SheffieldKrebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of SheffieldKrebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of SheffieldKrebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of SheffieldKrebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of SheffieldKrebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of SheffieldKrebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of SheffieldManchester Institute of Biotechnology and School of Chemistry, The University of ManchesterKrebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffieldβ-phosphoglucomutase (βPGM) from Lactococcus lactis is a phosphoryl transfer enzyme required for catabolism of trehalose and maltose. Coupled analyses of multiple βPGM structures and enzymatic activity lead to the proposal of allomorphy — a post-translational mechanism controlling enzyme activity.https://doi.org/10.1038/s41467-020-19215-9
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Henry P. Wood F. Aaron Cruz-Navarrete Nicola J. Baxter Clare R. Trevitt Angus J. Robertson Samuel R. Dix Andrea M. Hounslow Matthew J. Cliff Jonathan P. Waltho
spellingShingle	Henry P. Wood F. Aaron Cruz-Navarrete Nicola J. Baxter Clare R. Trevitt Angus J. Robertson Samuel R. Dix Andrea M. Hounslow Matthew J. Cliff Jonathan P. Waltho Allomorphy as a mechanism of post-translational control of enzyme activity Nature Communications
author_facet	Henry P. Wood F. Aaron Cruz-Navarrete Nicola J. Baxter Clare R. Trevitt Angus J. Robertson Samuel R. Dix Andrea M. Hounslow Matthew J. Cliff Jonathan P. Waltho
author_sort	Henry P. Wood
title	Allomorphy as a mechanism of post-translational control of enzyme activity
title_short	Allomorphy as a mechanism of post-translational control of enzyme activity
title_full	Allomorphy as a mechanism of post-translational control of enzyme activity
title_fullStr	Allomorphy as a mechanism of post-translational control of enzyme activity
title_full_unstemmed	Allomorphy as a mechanism of post-translational control of enzyme activity
title_sort	allomorphy as a mechanism of post-translational control of enzyme activity
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2020-11-01
description	β-phosphoglucomutase (βPGM) from Lactococcus lactis is a phosphoryl transfer enzyme required for catabolism of trehalose and maltose. Coupled analyses of multiple βPGM structures and enzymatic activity lead to the proposal of allomorphy — a post-translational mechanism controlling enzyme activity.
url	https://doi.org/10.1038/s41467-020-19215-9
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Allomorphy as a mechanism of post-translational control of enzyme activity

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