Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis

•Nucleotide-glucose synthesis in Mycobacterium tuberculosis was analyzed.•The characterization of four enzymes involved in glucose-1P partitioning is reported.•Mycobacterial ADP-glucose pyrophosphorylase is allosterically regulated.•Trehalose-6P synthase exhibits higher catalytic efficiency for ADP-...

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Main Authors:	Asención Diez, Matías D., Demonte, Ana M., Syson, Karl, Arias, Diego G., Gorelik, Andrii, Guerrero, Sergio A., Bornemann, Stephen, Iglesias, Alberto A.
Format:	Online
Language:	English
Published:	Elsevier Pub. Co 2015
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4331664/

id	pubmed-4331664
recordtype	oai_dc
spelling	pubmed-43316642015-03-03 Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis Asención Diez, Matías D. Demonte, Ana M. Syson, Karl Arias, Diego G. Gorelik, Andrii Guerrero, Sergio A. Bornemann, Stephen Iglesias, Alberto A. Article •Nucleotide-glucose synthesis in Mycobacterium tuberculosis was analyzed.•The characterization of four enzymes involved in glucose-1P partitioning is reported.•Mycobacterial ADP-glucose pyrophosphorylase is allosterically regulated.•Trehalose-6P synthase exhibits higher catalytic efficiency for ADP-glucose.•Trehalose-6P synthase is activated by fructose-6P. Elsevier Pub. Co 2015-01 /pmc/articles/PMC4331664/ /pubmed/25277548 http://dx.doi.org/10.1016/j.bbagen.2014.09.023 Text en © 2014 The Authors. Published by Elsevier B.V.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Asención Diez, Matías D. Demonte, Ana M. Syson, Karl Arias, Diego G. Gorelik, Andrii Guerrero, Sergio A. Bornemann, Stephen Iglesias, Alberto A.
spellingShingle	Asención Diez, Matías D. Demonte, Ana M. Syson, Karl Arias, Diego G. Gorelik, Andrii Guerrero, Sergio A. Bornemann, Stephen Iglesias, Alberto A. Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis
author_facet	Asención Diez, Matías D. Demonte, Ana M. Syson, Karl Arias, Diego G. Gorelik, Andrii Guerrero, Sergio A. Bornemann, Stephen Iglesias, Alberto A.
author_sort	Asención Diez, Matías D.
title	Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis
title_short	Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis
title_full	Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis
title_fullStr	Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis
title_full_unstemmed	Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis
title_sort	allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in mycobacterium tuberculosis
description	•Nucleotide-glucose synthesis in Mycobacterium tuberculosis was analyzed.•The characterization of four enzymes involved in glucose-1P partitioning is reported.•Mycobacterial ADP-glucose pyrophosphorylase is allosterically regulated.•Trehalose-6P synthase exhibits higher catalytic efficiency for ADP-glucose.•Trehalose-6P synthase is activated by fructose-6P.
publisher	Elsevier Pub. Co
publishDate	2015
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4331664/
_version_	1613189446015909888

Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis

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