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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Autores principales:	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
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b567dab9609e4747a1dcd185585f388f
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spelling	oai:doaj.org-article:b567dab9609e4747a1dcd185585f388f2021-12-02T15:39:12ZAllomorphy as a mechanism of post-translational control of enzyme activity10.1038/s41467-020-19215-92041-1723https://doaj.org/article/b567dab9609e4747a1dcd185585f388f2020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19215-9https://doaj.org/toc/2041-1723β-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.Henry P. WoodF. Aaron Cruz-NavarreteNicola J. BaxterClare R. TrevittAngus J. RobertsonSamuel R. DixAndrea M. HounslowMatthew J. CliffJonathan P. WalthoNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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
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.
format	article
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
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 Portfolio
publishDate	2020
url	https://doaj.org/article/b567dab9609e4747a1dcd185585f388f
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Allomorphy as a mechanism of post-translational control of enzyme activity

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