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5.4.99.16: maltose alpha-D-glucosyltransferase

This is an abbreviated version!
For detailed information about maltose alpha-D-glucosyltransferase, go to the full flat file.

Word Map on EC 5.4.99.16

Reaction

maltose
=
alpha,alpha-trehalose

Synonyms

57-KDa trehalose synthase (Saccharomyces cerevisiae), Dgeo_0537, DKY63_02445, DOT40_01605, DrTreS, DrTS, DR_2036, FM102_08285, HMPREF9086_3732, Maltose alpha-D-glucosylmutase, Maltose alpha-D-glucosyltransferase, Maltose glucosylmutase, MTase, MtTS, Protein (Saccharomyces cerevisiae clone pMB14 gene CIF reduced), Protein (Saccharomyces cerevisiae gene CIF1 reduced), PTO0069, PTTS, Synthase, trehalose, Synthase, trehalose (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced), Synthase, trehalose (Saccharomyces cerevisiae gene TPS1 subunit), Synthase, trehalose (Saccharomyces cerevisiae gene TSL1 subunit), Synthase, trehalose (Thermus aquaticus strain ATCC33923 clone pBTM5), TaTS, Tfu_0584, Trehalose synthase, Trehalose synthase (Pimelobacter strain R48 clone pBRM8 gene treS precursor reduced), Trehalose synthetase, TreS, treSB, TSase, Tter_0330, TtTreS, TtTS

ECTree

     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.16 maltose alpha-D-glucosyltransferase

Crystallization

Crystallization on EC 5.4.99.16 - maltose alpha-D-glucosyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme complexed with Ca2+, Mg2+, and tromethamine, PDB ID 4TVU, X-ray diffraction structure determination and analysis at 2.7 A resolution
purified recombinant enzyme mutant N253F, hanging drop vapour diffusion method, mixing of 0.002 ml of 30 mg/ml protein in 20 mM HEPES, pH 7.5, 100 mM NaCl, 3.3% glycerol, and 1 mM DTT, with 0.0.02 ml of reservoir solution containing 0.3 M Tris-HCl pH 7.0, 7% PEG 4000, and 0.2 M sodium acetate trihydrate, and equilibration against 0.5 ml of reservoir solution, 15°C, 2-3 weeks, X-ray diffraction structure determination and analysis
purified recombinant wild-type and N253A mutant enzymes in complex with inhibitor Tris, hanging drop vapour diffusion method, 15°C, for the wild-type enzyme, mixing of 0.002 ml of 30 mg/ml protein in 20 mM sodium phosphate, pH 7.4, with 0.002 ml of reservoir solution containing 9% PEG 4000, 0.2 M sodium acetate trihydrate, 0.3 M Tris-HCl, pH 8.5, 6-8 weeks, for the mutant enzyme, mixing of 0.002 ml of 60 mg/ml protein in 20 mM sodium phosphate, pH 7.4, with 0.002 ml of reservoir solution containing 11% PEG 4000, 0.2 M sodium acetate trihydrate, 0.3 M Tris-HCl, pH 8.5, and 5% glycerol, 2 weeks, X-ray diffracion structure determination and analysis at 2.21-2.70 A resolution
enzyme complexed with Ca2+, glycerin, and sulfate ion, PDB ID 4LXF, X-ray diffraction structure determination and analysis at 2.6 A resolution
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
enzyme complexed with alpha-acarbose, Ca2+, Cl-, and Mg2+ or with Cl-, Ca2+, and Mg2+, PDB IDs 3ZOA and 3ZO9, X-ray diffraction structure determination and analysis at 1.85 and 1.84 A resolution, respectively
free enzyme and enzyme in complex with inhibitor acarbose, hanging drop vapor diffusion technique, mixing of 0.002 ml of 20 mg/ml protein in 40 mM sodium phosphate buffer, pH 6.0, with 0.002 ml of reservoir solution containing 0.1 M sodium cacodylate, pH 6.5, 0.2 M MgCl2, and 10-14% PEG 1000, 20°C, 1 day to 1 week, X-ray diffraction structure determination and analysis at 1.84 A resolution, molecular replacement
enzyme, PDB ID 5X7U, X-ray diffraction structure determination and analysis at 2.5 A resolution