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Results 1 - 9 of 9
EC Number
Subunits
Commentary
Reference
?
x * 35600, SDS-PAGE
?
x * 61315, calculation from amino acid sequence; x * 80000, SDS-PAGE
dimer
2 * 82000, SDS-PAGE
hexamer
6 * 36000, recombinant enzyme, SDS-PAGE
hexamer
crystallographic data
hexamer
the relevant physiological oligomeric state of the enzyme is a hexamer, in the crystal structure, two hexamers in the asymmetric unit, that are related by a non-crystallographic two-fold axis, contain each a dimer of trimers with a back-to-back arrangement, enzyme quaternary structure, overview. Two main interfaces play an essential role in complex formation, the first interface between subunit A and B, and he second interface between A and F. The entrance to the internal cavity is blocked by three phenylalanine residues (Phe4), one for each of three monomers that compose half of the hexamer
octamer
8 * 35000, strain SHS 0133, SDS-PAGE
octamer
8 * 35000, strain SHS 0133, SDS-PAGE; 8 * 35000, strain SHS 0133, SDS-PAGE
-
tetramer
strain ATCC6633
Results 1 - 9 of 9