A FUNCTIONAL ROLE OF METAL IONS IN A CLASS 2 ALDOLASE

被引:86
作者
KOBES, RD
SIMPSON, RT
VALLEE, BL
RUTTER, WJ
机构
[1] Department of Biochemistry, University of Washington, Seattle
关键词
D O I
10.1021/bi00830a018
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A crucial role of the metal ion in the catalytic activity of yeast aldolase has been demonstrated. Zinc can be removed from the native enzyme resulting in an inactive apoenzyme. The activity can be reconstituted by addition of Zn2+ or by certain ions of the first transition period, namely C2+, Ni2+, Mn2+, and Fe2+. The Zn2+ protein has thehighest specific activity; the other metal ions restore the enzymatic activity to varying de grees.A number of other metal ions (Cu2+, Hg2+, Cd2+, Mg2+, and Fe3+) fail to restore activity to any measurable extent. All active metalloaldolases exhibit similar Km values for fructose diphosphate and are stimulated by K+ ion. © 1969, American Chemical Society. All rights reserved.
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页码:585 / &
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