Limited proteolysis of Hansenula polymorpha yeast amine oxidase: isolation of a C-terminal fragment containing both a copper and quino-cofactor.
Limited proteolysis of recombinant Hansenula polymorpha yeast amino oxidase produces a 48 kDa fragment which corresponds to the C-terminal two-thirds of the protein. The fragment contains both TOPA (2,4,5-trihydroxyphenylalanine) and copper, as well as the histidine ligands implicated in copper binding. The fragment is proposed to be the domain responsible for cofactor production in yeast amine oxidase.
Plastino
J
J
Department of Chemistry, University of California, Berkeley 94720, USA.
Klinman
J P
JP
D006631:Amine Oxidase (Copper-Containing); D003067:Coenzymes / Q000032:analysis; D003300:Copper / Q000032:analysis; D004295:Dihydroxyphenylalanine / Q000031:analogs & derivatives / Q000032:analysis; D006639:Histidine; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000737:chemistry*; D010843:Pichia / Q000201:enzymology*; D012697:Serine Endopeptidases
D003067:Coenzymes; C001388:6-hydroxydopa; D006639:Histidine; D004295:Dihydroxyphenylalanine; D003300:Copper; D006631:Amine Oxidase (Copper-Containing); D000587:Oxidoreductases Acting on CH-NH Group Donors; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase