Activity of yeast orotidine-5'-phosphate decarboxylase in the absence of metals.
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.
Miller
B G
BG
Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260, USA.
Smiley
J A
JA
Short
S A
SA
Wolfenden
R
R
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*
D011994:Recombinant Proteins; D009964:Orotidine-5'-Phosphate Decarboxylase; D015032:Zinc