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Literature summary extracted from

  • Wohlfahrt, G.; Witt, S.; Hendle, J.; Schomburg, D.; Kalisz, H.M.; Hecht, H.J.
    1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes (1999), Acta Crystallogr. Sect. D, 55, 969-977.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.3.4 structure refined at 1.9 A resolution to an R value of 19.0% Aspergillus niger
1.1.3.4 the enzyme crystallizes from 1.3 M ammonium sulfate, 100 mM citrate/phosphate buffer pH 7.4 in the orthorhombic space group P212121, with unit-cell dimensions a = 57.6, b = 132.1, c = 151.3 A and one dimeric molecule per asymmetric unit. The structure is determined by molecular replacement and refined at 1.8 A resolution to an R value of 16.4% Penicillium amagasakiense

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.4 Aspergillus niger P13006
-
-
1.1.3.4 Penicillium amagasakiense P81156
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.4
-
Aspergillus niger
1.1.3.4
-
Penicillium amagasakiense

Synonyms

EC Number Synonyms Comment Organism
1.1.3.4 GOX
-
Aspergillus niger
1.1.3.4 GOX
-
Penicillium amagasakiense