Structural Insight into How Streptomyces coelicolor Maltosyl Transferase GlgE Binds α-Maltose 1-Phosphate and Forms a Maltosyl-enzyme Intermediate-Reference-Cited by-同舟云学术

Structural Insight into How Streptomyces coelicolor Maltosyl Transferase GlgE Binds α-Maltose 1-Phosphate and Forms a Maltosyl-enzyme Intermediate

Published:2014-04-11 Issue:15 Volume:53 Page:2494-2504
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Syson Karl¹,Stevenson Clare E. M.¹,Rashid Abdul M.¹,Saalbach Gerhard¹,Tang Minhong¹,Tuukkanen Anne²,Svergun Dmitri I.²,Withers Stephen G.³,Lawson David M.¹,Bornemann Stephen¹

Affiliation:

1. Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom

2. Hamburg Outstation, European Molecular Biology Laboratory, c/o DESY, 22603 Hamburg, Germany

3. Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z1

Funder

Biotechnology and Biological Sciences Research Council

European Commission

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi500183c

Reference51 articles.

1. Self-poisoning of Mycobacterium tuberculosis by targeting GlgE in an α-glucan pathway

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

3. Mycobacterium tuberculosis Maltosyltransferase GlgE, a Genetically Validated Antituberculosis Target, Is Negatively Regulated by Ser/Thr Phosphorylation

4. Unexpected and widespread connections between bacterial glycogen and trehalose metabolism

5. The challenge of new drug discovery for tuberculosis

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