A specific enzyme for glucose 1,6-bisphosphate synthesis

J Biol Chem. 1975 May 10;250(9):3466-70.


The reaction: glycerate-1,3-P2 PLUS GLUCOSE-1-P YIELDS TO GLUCOSE-1,6-P2 plus glycerate-P is catalyzed by a distinct enzyme of mouse brain. A divalent metal requirement was shown when the enzyme was treated with imidazole and EDTA. Mg2+, Mn2+, Ca2+, Zn2+, Ni2+, Co2+, and Cd2+ were quite effective cofactors. The enzyme, in better than 50 percent yield, has been purified away from 99 percent of the phosphoglucomutase, phosphoglycrate mutase, and phosphofructokinase. Acetyl-P, ATP, enolpyruvate-P, creatine-P, and fructose-1,6-P2 are not phosphoryl donors. Glucose-6-P and mannose-1-P are good alternate acceptors. Mannose-6-P, galactose-Ps, and fructose-Ps have little or no acceptor activity. Strong inhibition was found with fructose-1,6-P2, glycerate-2,3-P2, enolpyruvate-P, and acetyl CoA. From the amount of activity and the kinetic constants of the purified enzyme it seems likely that this enzyme is responsible for the glucose-1,6-P2 synthesis of brain.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acetyl Coenzyme A / pharmacology
  • Animals
  • Brain / enzymology*
  • Cations, Divalent / pharmacology
  • Diphosphoglyceric Acids / metabolism
  • Fructosephosphates / pharmacology
  • Glucosephosphates / biosynthesis*
  • Hexosediphosphates / biosynthesis*
  • Hydrogen-Ion Concentration
  • Kinetics
  • Mannose / metabolism
  • Mice
  • Phosphoenolpyruvate / pharmacology
  • Phosphotransferases / metabolism*


  • Cations, Divalent
  • Diphosphoglyceric Acids
  • Fructosephosphates
  • Glucosephosphates
  • Hexosediphosphates
  • Acetyl Coenzyme A
  • Phosphoenolpyruvate
  • Phosphotransferases
  • Mannose