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Purification and characteristics of DOPA-decarboxylase from the integument of Calliphora vicina larve

1975; Elsevier BV; Volume: 168; Issue: 1 Linguagem: Inglês

10.1016/0003-9861(75)90223-4

1096-0384

Emmanuel G. Fragoulis, Constantin E. Sekeris,

Coenzyme Q10 studies and effects

A method is described for the purification to homogeneity of the DOPA-decarboxylase present in the integument of blowfly larve. The enzyme has a Mr of 90,000–96,000 and is composed of two subunits of Mr 50,000 and 46,000. The enzyme decarboxylates DOPA and is practically inactive towards 5-hydroxytryptophan, tryptophan, tyrosine, and phenylalanine. Enzyme activity is enhanced by Al3+ and Mn2+ and is depressed by Cu2+ and Hg2+. N-Acetyldopamine is a competitive inhibitor of the decarboxylase.