3.1.1.41	?	x * 35600, SDS-PAGE	752071	
3.1.1.41	?	x * 61315, calculation from amino acid sequence	170675	
3.1.1.41	?	x * 80000, SDS-PAGE	170675	
3.1.1.41	dimer	2 * 82000, SDS-PAGE	-, 170672	
3.1.1.41	hexamer	6 * 36000, recombinant enzyme, SDS-PAGE	-, 729073	
3.1.1.41	hexamer	crystallographic data	652917	
3.1.1.41	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	730907	
3.1.1.41	octamer	8 * 35000, strain SHS 0133, SDS-PAGE	-, 170673, 170677	
3.1.1.41	tetramer	strain ATCC6633	-, 170673