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Literature summary extracted from

  • Kobayashi, M.; Kubota, M.; Matsuura, Y.
    Crystallization and improvement of crystal quality for X-ray diffraction of maltooligosyl trehalose synthase by reductive methylation of lysine residues (1999), Acta Crystallogr. Sect. D, 55, 931-933.
No PubMed abstract available

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
5.4.99.15 hanging-drop vapour-diffusion method at 4°C. The chemical modification of this enzyme by reductive methylation of lysine residues significantly improves the crystal quality for X-ray diffraction experiments. The crystals of the modified enzyme belong to orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 56.70, b = 140.1, c = 205.2 A measured at cryo-temperature, and are found to contain two enzyme molecules per asymmetric unit Sulfolobus acidocaldarius
5.4.99.15 recombinant enzyme expressed in Escherichia coli, hanging-drop vapour-diffusion method, chemical modification of this enzyme by reductive methylation of lysine residues significantly improves the crystal quality for X-ray diffraction experiments Sulfolobus acidocaldarius

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.15 Sulfolobus acidocaldarius
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.4.99.15
-
 Sulfolobus acidocaldarius
5.4.99.15 recombinant enzyme expressed in Escherichia coli Sulfolobus acidocaldarius

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.15 alpha-maltotriosyl trehalose
-
 Sulfolobus acidocaldarius maltopentaose
-
 ?

Synonyms

EC Number Synonyms Comment Organism
5.4.99.15 maltooligosyl trehalose synthase
-
 Sulfolobus acidocaldarius
5.4.99.15 MTSase
-
 Sulfolobus acidocaldarius