title: Activity of yeast orotidine-5'-phosphate decarboxylase in the absence of metals.
abstract: Yeast orotidine-5'-phosphate decarboxylase was recently shown to contain zinc and to be inhibited by zinc-complexing agents. When the gene for the yeast enzyme was expressed in Escherichia coli, the gene product was devoid of metal atoms but exhibited a specific activity and molecular mass similar to those of the enzyme obtained directly from yeast. This invalidates the hypothesis that zinc is involved in substrate decarboxylation. The zinc-free enzyme undergoes thermal inactivation at a somewhat lower temperature than does the zinc-containing enzyme isolated from yeast.
authors.affiliation: Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260, USA.
authors.forename: B G
authors.initials: BG
authors.lastname: Miller
authors.forename: J A
authors.initials: JA
authors.lastname: Smiley
authors.forename: S A
authors.initials: SA
authors.lastname: Short
authors.forename: R
authors.initials: R
authors.lastname: Wolfenden
mesh_terms: D004926:Escherichia coli / Q000235:genetics; D009964:Orotidine-5'-Phosphate Decarboxylase / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D015003:Yeasts / Q000201:enzymology*; D015032:Zinc / Q000502:physiology*
chemical_list: D011994:Recombinant Proteins; D009964:Orotidine-5'-Phosphate Decarboxylase; D015032:Zinc