FRUCTOSE-1,6-DIPHOSPHATASE OF ACINETOBACTER - INHIBITION BY ATP AND CITRATE

被引:6
作者
MUKKADA, AJ
BELL, EJ
机构
[1] Department of Biological Sciences, the Graduate Division of Microbiology, University of Cincinnati, Cincinnati
关键词
D O I
10.1016/0006-291X(69)90740-2
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
Fructose-1,6-diphosphatase (FDPase) from a species of Acinetobacter was partially purified and some of its properties studied. The enzyme resembles other FDPases investigated in its dependence on a divalent metal like Mg++ or Mn++, high affinity for the substrate, stimulation by EDTA and inhibition by high substrate concentrations. However, it differs from most other FDPases in its insensitivity to AMP and inhibition by ATP and citrate. © 1969.
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页码:340 / &
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