Anomeric specificity of the alkaline form of fructose 1,6 diphosphatase from rabbit liver

Patricia Ann Benkovic, W. P. Bullard, M. de Maine, R. Fishbein, K. J. Schray, J. J. Steffens, Stephen Benkovic

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Abstract

The preferred configuration of the active substrate for rabbit liver fructose 1,6 diphosphatase has been determined by techniques based on rapid quench kinetics to be the α anomer of fructose 1,6 P 2. Utilization of the β anomer, however, is also catalyzed by the enzyme with a rate coefficient 5 to 10 fold less than that for the α anomer.

Original languageEnglish (US)
Pages (from-to)930-931
Number of pages2
JournalJournal of Biological Chemistry
Volume249
Issue number3
Publication statusPublished - Jan 1 1974

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All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Benkovic, P. A., Bullard, W. P., de Maine, M., Fishbein, R., Schray, K. J., Steffens, J. J., & Benkovic, S. (1974). Anomeric specificity of the alkaline form of fructose 1,6 diphosphatase from rabbit liver. Journal of Biological Chemistry, 249(3), 930-931.