Title Purification and Characteristics of 3-Deoxy-D-arabino-heptulosonate-7-phosphate Synthetase from Streptomyces caespitosus
Author Yoom Jin Cheol * · Bang, hee Jae · Lee, Eun Ha¹ · Kim, Sung Jun¹ · Lee, Jung Jun²
Address Department of Pharmacy;¹Department of Genetic Engineering, Chosun University; ²Genetic Engineering Research Institute, KIST
Bibliography Korean Journal of Microbiology, 31(4),340-345, 1993
Key Words Streptomyces caespitosus, DAHP synthetase
Abstract 3-Deoxy-D-arabino-heptulosonate-7-phosphate(DAHP) synthetase, the first enzyme of the shikimate pathway was purified to near homogeneity from Streptomyces caespitosus. It had a molecular weight of approximately 56,000 daltons on SDS-PAGE and Sephadex G-150 gel filtration. The K-m values for phosphoenolpyruvate(PEP) and D-erythrose-4-phosphate(E-4-P) were 0.43 mM and 0.22 mM, respectively. The pH and temperature for maximum enzyme activity were 7.2 and 37℃. Treatment with ethylenediamine-tetraacetic acid(EDTA) removed 80% of the activity of the enzyme. This activity was restored upon the addition of Co^2+ ion and partially restored upon the addition of Zn^2+ or Mn^2+ ion. But, Ni62+, Fe^2+ and Ca^2+ ions inhibited activity of the DAHP synthetase from S. caespitosus.
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