Biochemical studies on inositol. VIII. Purification and properties of the enzyme system which converts glucose-6-phosphate to inositol

Chen; Charalampous, F.C.

Journal of Biological Chemistry 240(9): 3507-3512

1965


ISSN/ISBN: 0021-9258
Accession: 024239132

Download citation:  
Text
  |  
BibTeX
  |  
RIS

Article/Abstract emailed within 1 workday
Payments are secure & encrypted
Powered by Stripe
Powered by PayPal

Abstract
The enzyme system of Candida utilis Y-900 which catalyzes the conversion of glucose-6-phosphate to inositol was purified 100-fold. The purified system was shown to require DPN and Mg++ ions, while NH4 + ions accelerated the reaction rate 5-fold. Other known coenzymes could not substitute for DPN. During the biosynthesis of inositol from glucose-6-P DPN is reduced, and the kinetics exhibited 2 distinct linear rates, a fast one lasting for 5 minutes, and a slower one lasting for 1 hour. The enzyme system was inhibited by heavy metals, potassium fluoride, sulfhydryl reagents, and various phosphorylated compounds. By the use of variously labeled C14-glucose-6-P followed by degradation of the synthesized radioactive inositols it was possible to demonstrate that glucose-6-P is used as an intact 6 carbon unit.