Literature summary for 5.4.99.16 extracted from

Kermani, A.; Roy, R.; Gopalasingam, C.; Kocurek, K.; Patel, T.; Alderwick, L.; Besra, G.; F�tterer, K.
Crystal structure of the TreS Pep2 complex, initiating a-glucan synthesis in the GlgE pathway of mycobacteria (2019), J. Biol. Chem., 294, 7348-7359 .

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Mycolicibacterium smegmatis

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals are grown by vapor diffusion. Structure of the Mycobacterium smegmatis TreS:Pep2 complex, containing trehalose synthase (TreS) and maltokinase (Pep2), which converts trehalose to maltose 1-phosphate as part of the TreS:Pep2-GlgE pathway. The structure, at 3.6 A resolution, reveals that a diamond-shaped TreS tetramer forms the core of the complex and that pairs of Pep2 monomers bind to opposite apices of the tetramer in a 4 + 4 configuration	Mycolicibacterium smegmatis

Crystallization (Comment)

Organism

crystals are grown by vapor diffusion. Structure of the Mycobacterium smegmatis TreS:Pep2 complex, containing trehalose synthase (TreS) and maltokinase (Pep2), which converts trehalose to maltose 1-phosphate as part of the TreS:Pep2-GlgE pathway. The structure, at 3.6 A resolution, reveals that a diamond-shaped TreS tetramer forms the core of the complex and that pairs of Pep2 monomers bind to opposite apices of the tetramer in a 4 + 4 configuration

Mycolicibacterium smegmatis

Organism

Organism	UniProt	Comment	Textmining
Mycolicibacterium smegmatis	A0R6E0	-	-
Mycolicibacterium smegmatis ATCC 700084	A0R6E0	-	-

Synonyms

Synonyms	Comment	Organism
TreS	-	Mycolicibacterium smegmatis

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Release 2023.1 (January 2023)