Anomeric specificity of phosphofructokinase from rabbit muscle

R. Fishbein, P. A. Benkovic, K. J. Schray, I. J. Siewers, J. J. Steffens, S. J. Benkovic

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

Rabbit muscle phosphofructokinase apparently utilizes only the β furanose anomer as disclosed by rapid quench kinetic studies employing D fructose 6 P and D tagatose 6 P. Approximately 80% of the substrate, a figure that closely corresponds to the percentage β anomer, is converted to the diphosphate in a rapid initial phase. Investigations utilizing methyl α,β D fructofuranoside 6 P as a substrate analog demonstrated exclusive phosphorylation of the β anomer to yield methyl β D fructofuranoside 1,6 P 2. The occurrence of fructoside phosphorylation argues against the need for an intervening keto form to accomplish the transphosphorylation process. An absolute stereoselectivity of phosphofructokinase for the β anomer of fructose 6 P thus is indicated.

Original languageEnglish (US)
Pages (from-to)6047-6051
Number of pages5
JournalJournal of Biological Chemistry
Volume249
Issue number19
StatePublished - Dec 1 1974

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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