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Literature summary for 3.2.1.78 extracted from

  • Santos, C.R.; Squina, F.M.; Navarro, A.M.; Ruller, R.; Prade, R.; Murakami, M.T.
    Cloning, expression, purification, crystallization and preliminary X-ray diffraction studies of the catalytic domain of a hyperthermostable endo-1,4-beta-D-mannanase from Thermotoga petrophila RKU-1 (2010), Acta Crystallogr. Sect. F, 66, 1078-1081.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Thermotoga petrophila

Crystallization (Commentary)

Crystallization (Comment) Organism
crystallization of catalytic domain. Crystals from conditions with phosphate or citrate salts as precipitant belong to space group P212121, resolution to 1.4 A, while a crystal from a condition with ethanol as precipitant belongs to space group I212121, resolution to 1.45 A Thermotoga petrophila

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44000
-
x * 44000, SDS-PAGE Thermotoga petrophila

Organism

Organism UniProt Comment Textmining
Thermotoga petrophila A5IMX7
-
-
Thermotoga petrophila RKU-1 A5IMX7
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermotoga petrophila

Subunits

Subunits Comment Organism
? x * 44000, SDS-PAGE Thermotoga petrophila