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Literature summary extracted from

  • Kermani, A.; Roy, R.; Gopalasingam, C.; Kocurek, K.; Patel, T.; Alderwick, L.; Besra, G.; Fütterer, 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 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.16
-
 Mycolicibacterium smegmatis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.175 purified recombinant TreS:Pep2 complex, containing trehalose synthase (TreS) and maltokinase (Pep2), X-ray diffraction structure determination and analysis at 3.6 A resolution Mycolicibacterium smegmatis
5.4.99.16 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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.175 additional information
-
 additional information kinetics analysis of the TreS:Pep2 complex activity, overview Mycolicibacterium smegmatis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.175 Mg2+ required Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.175 ATP + maltose Mycolicibacterium smegmatis
-
 ADP + alpha-maltose-1-phosphate
-
 ?
2.7.1.175 ATP + maltose Mycolicibacterium smegmatis ATCC 700084
-
 ADP + alpha-maltose-1-phosphate
-
 ?
2.7.1.175 ATP + maltose Mycolicibacterium smegmatis mc(2)155
-
 ADP + alpha-maltose-1-phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.175 Mycolicibacterium smegmatis A0R6D9 Mycobacterium smegmatis
-
2.7.1.175 Mycolicibacterium smegmatis ATCC 700084 A0R6D9 Mycobacterium smegmatis
-
2.7.1.175 Mycolicibacterium smegmatis mc(2)155 A0R6D9 Mycobacterium smegmatis
-
5.4.99.16 Mycolicibacterium smegmatis A0R6E0
-
-
5.4.99.16 Mycolicibacterium smegmatis ATCC 700084 A0R6E0
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.175 ATP + maltose
-
 Mycolicibacterium smegmatis ADP + alpha-maltose-1-phosphate
-
 ?
2.7.1.175 ATP + maltose
-
 Mycolicibacterium smegmatis ATCC 700084 ADP + alpha-maltose-1-phosphate
-
 ?
2.7.1.175 ATP + maltose
-
 Mycolicibacterium smegmatis mc(2)155 ADP + alpha-maltose-1-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.175 More in the TreS:Pep2 complex crystal, diamond-shaped TreS tetramer forms the core of the complex and pairs of Pep2 monomers bind to opposite apices of the tetramer in a 4 + 4 configuration, but the prevalent stoichiometry in solution is 4 TreS + 2 Pep2 protomers. The behavior in the solution state may be explained by the relatively weak affinity of Pep2 for TreS (Kd 3.5 microM at mildly acidic pH) and crystal packing favoring the 4 + 4 complex. Pep2 forms intimate contacts with the TreS tetramer, revealing a high level of shape complementarity between the binding partners. Structure model, overview. Secondary structure elements contributing to the binding interface are helices alpha5, alpha6, and alpha10 in the C-terminal lobe of Pep2, and contacts made by the N-terminal lobe include residues in helix alpha2, in strand beta8, and in the beta9-beta10 loop. In addition, contacts also involve the beta12-alpha5 loop, which links the N- and C-terminal lobes. The binding interface is dominated by van der Waals and hydrophobic contacts, corresponding to about 70% of surface area buried in the interface per Pep2 monomer Mycolicibacterium smegmatis

Synonyms

EC Number Synonyms Comment Organism
2.7.1.175 Msm Pep2
-
 Mycolicibacterium smegmatis
2.7.1.175 Pep2
-
 Mycolicibacterium smegmatis
5.4.99.16 TreS
-
 Mycolicibacterium smegmatis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.175 6
-
 assay at Mycolicibacterium smegmatis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.175 ATP
-
 Mycolicibacterium smegmatis

General Information

EC Number General Information Comment Organism
2.7.1.175 metabolism the enzyme is part of the Mycobacterium smegmatis TreS:Pep2 complex, containing trehalose synthase (TreS, EC 2.4.1.245) and maltokinase (Pep2), which converts trehalose to maltose 1-phosphate as part of the TreS:Pep2-GlgE pathway. Proximity of the ATP-binding site in Pep2 to the complex interface provides a rational basis for rate enhancement of Pep2 upon binding to TreS, but the complex structure appears to rule out substrate channeling between the active sites of TreS and Pep2 Mycolicibacterium smegmatis
2.7.1.175 additional information enzyme complex structure analysis and location of active sites, overview Mycolicibacterium smegmatis
2.7.1.175 physiological function the enzyme is part of the Mycobacterium smegmatis TreS:Pep2 complex, containing trehalose synthase (TreS, EC 2.4.1.245) and maltokinase (Pep2), which converts trehalose to maltose 1-phosphate as part of the TreS:Pep2-GlgE pathway. Proximity of the ATP-binding site in Pep2 to the complex interface provides a rational basis for rate enhancement of Pep2 upon binding to TreS, but the complex structure appears to rule out substrate channeling between the active sites of TreS and Pep2 Mycolicibacterium smegmatis