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Literature summary for 2.7.1.175 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
Search for more literature for 2.7.1.175

Crystallization (Commentary)

Crystallization (Comment) Organism
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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Mycolicibacterium smegmatis

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis A0R6D9 Mycobacterium smegmatis
-
Mycolicibacterium smegmatis ATCC 700084 A0R6D9 Mycobacterium smegmatis
-
Mycolicibacterium smegmatis mc(2)155 A0R6D9 Mycobacterium smegmatis
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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

Synonyms Comment Organism
Msm Pep2
-
 Mycolicibacterium smegmatis
Pep2
-
 Mycolicibacterium smegmatis

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Mycolicibacterium smegmatis

General Information

General Information Comment Organism
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
additional information enzyme complex structure analysis and location of active sites, overview Mycolicibacterium smegmatis
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