Flux through Trehalose Synthase Flows from Trehalose to the Alpha Anomer of Maltose in Mycobacteria

Trehalose synthase (TreS) was thought to catalyze flux from maltose to trehalose, a precursor of essential trehalose mycolates in mycobacterial cell walls. However, we now show, using a genetic approach, that TreS is not required for trehalose biosynthesis in Mycobacterium smegmatis, whereas two alt...

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Main Authors:	Miah, Farzana, Koliwer-Brandl, Hendrik, Rejzek, Martin, Field, Robert A., Kalscheuer, Rainer, Bornemann, Stephen
Format:	Online
Language:	English
Published:	Elsevier 2013
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3918855/

id	pubmed-3918855
recordtype	oai_dc
spelling	pubmed-39188552014-02-10 Flux through Trehalose Synthase Flows from Trehalose to the Alpha Anomer of Maltose in Mycobacteria Miah, Farzana Koliwer-Brandl, Hendrik Rejzek, Martin Field, Robert A. Kalscheuer, Rainer Bornemann, Stephen Brief Communication Trehalose synthase (TreS) was thought to catalyze flux from maltose to trehalose, a precursor of essential trehalose mycolates in mycobacterial cell walls. However, we now show, using a genetic approach, that TreS is not required for trehalose biosynthesis in Mycobacterium smegmatis, whereas two alternative trehalose-biosynthetic pathways (OtsAB and TreYZ) are crucial. Consistent with this direction of flux, trehalose levels in Mycobacterium tuberculosis decreased when TreS was overexpressed. In addition, TreS was shown to interconvert the α anomer of maltose and trehalose using 1H and 19F-nuclear magnetic resonance spectroscopies using its normal substrates and deoxyfluoromaltose analogs, with the nonenzymatic mutarotation of α/β-maltose being slow. Therefore, flux through TreS in mycobacteria flows from trehalose to α-maltose, which is the appropriate anomer for maltose kinase of the GlgE α-glucan pathway, which in turn contributes to intracellular and/or capsular polysaccharide biosynthesis. Elsevier 2013-04-18 /pmc/articles/PMC3918855/ /pubmed/23601637 http://dx.doi.org/10.1016/j.chembiol.2013.02.014 Text en © 2013 Elsevier Ltd. This document may be redistributed and reused, subject to certain conditions (http://www.elsevier.com/wps/find/authorsview.authors/supplementalterms1.0) .
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	Miah, Farzana Koliwer-Brandl, Hendrik Rejzek, Martin Field, Robert A. Kalscheuer, Rainer Bornemann, Stephen
spellingShingle	Miah, Farzana Koliwer-Brandl, Hendrik Rejzek, Martin Field, Robert A. Kalscheuer, Rainer Bornemann, Stephen Flux through Trehalose Synthase Flows from Trehalose to the Alpha Anomer of Maltose in Mycobacteria
author_facet	Miah, Farzana Koliwer-Brandl, Hendrik Rejzek, Martin Field, Robert A. Kalscheuer, Rainer Bornemann, Stephen
author_sort	Miah, Farzana
title	Flux through Trehalose Synthase Flows from Trehalose to the Alpha Anomer of Maltose in Mycobacteria
title_short	Flux through Trehalose Synthase Flows from Trehalose to the Alpha Anomer of Maltose in Mycobacteria
title_full	Flux through Trehalose Synthase Flows from Trehalose to the Alpha Anomer of Maltose in Mycobacteria
title_fullStr	Flux through Trehalose Synthase Flows from Trehalose to the Alpha Anomer of Maltose in Mycobacteria
title_full_unstemmed	Flux through Trehalose Synthase Flows from Trehalose to the Alpha Anomer of Maltose in Mycobacteria
title_sort	flux through trehalose synthase flows from trehalose to the alpha anomer of maltose in mycobacteria
description	Trehalose synthase (TreS) was thought to catalyze flux from maltose to trehalose, a precursor of essential trehalose mycolates in mycobacterial cell walls. However, we now show, using a genetic approach, that TreS is not required for trehalose biosynthesis in Mycobacterium smegmatis, whereas two alternative trehalose-biosynthetic pathways (OtsAB and TreYZ) are crucial. Consistent with this direction of flux, trehalose levels in Mycobacterium tuberculosis decreased when TreS was overexpressed. In addition, TreS was shown to interconvert the α anomer of maltose and trehalose using 1H and 19F-nuclear magnetic resonance spectroscopies using its normal substrates and deoxyfluoromaltose analogs, with the nonenzymatic mutarotation of α/β-maltose being slow. Therefore, flux through TreS in mycobacteria flows from trehalose to α-maltose, which is the appropriate anomer for maltose kinase of the GlgE α-glucan pathway, which in turn contributes to intracellular and/or capsular polysaccharide biosynthesis.
publisher	Elsevier
publishDate	2013
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3918855/
_version_	1612056611695624192

Flux through Trehalose Synthase Flows from Trehalose to the Alpha Anomer of Maltose in Mycobacteria

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