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Literature summary for 4.2.2.18 extracted from

  • Momma, M.; Fujimoto, Z.; Maita, N.; Haraguchi, K.; Mizuno, H.
    Expression, crystallization and preliminary X-ray crystallographic studies of Arthrobacter globiformis inulin fructotransferase (2003), Acta Crystallogr. Sect. D, D59, 2286-2288.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Arthrobacter globiformis

Crystallization (Commentary)

Crystallization (Comment) Organism
crystals are obtained at 20°C by hanging drop vapour-diffusion method using 0.1 M Na HEPES pH 7.5 buffer containing 1.5 M lithium sulfate as a precipitant. Crystals of the recombinant wild-type enzyme diffract to better than 1.5 A at -173°C. The crystals belong to space group R32, with unit-cell parameters a = b = 90.02 A, c = 229.82 A in the hexagonal axes. Selenomethionine-derivative crystals belong to a different space group, C2, with unit-cell parameters a = 159.32, cb = 91.92, c = 92.58 A, beta = 125.06. The C2 selenomethionine-derived crystal contains three molecules per asymmetric unit Arthrobacter globiformis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
43000
-
3 * 43000, SDS-PAGE Arthrobacter globiformis

Organism

Organism UniProt Comment Textmining
Arthrobacter globiformis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant Arthrobacter globiformis

Subunits

Subunits Comment Organism
trimer 3 * 43000, SDS-PAGE Arthrobacter globiformis

Synonyms

Synonyms Comment Organism
IFTaseIII
-
Arthrobacter globiformis
inulin fructotransferase (DFAIII-producing)
-
Arthrobacter globiformis