Anomeric specificity of phosphofructokinase from rabbit muscle

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

Research output: Contribution to journalArticle

22 Citations (Scopus)

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 - 1974

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Phosphofructokinases
Phosphorylation
Fructose
Muscle
Rabbits
Stereoselectivity
Muscles
Diphosphates
Substrates
Kinetics
tagatose

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Fishbein, R., Benkovic, P. A., Schray, K. J., Siewers, I. J., Steffens, J. J., & Benkovic, S. (1974). Anomeric specificity of phosphofructokinase from rabbit muscle. Journal of Biological Chemistry, 249(19), 6047-6051.
Fishbein, R. ; Benkovic, P. A. ; Schray, K. J. ; Siewers, I. J. ; Steffens, J. J. ; Benkovic, Stephen. / Anomeric specificity of phosphofructokinase from rabbit muscle. In: Journal of Biological Chemistry. 1974 ; Vol. 249, No. 19. pp. 6047-6051.
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Fishbein, R, Benkovic, PA, Schray, KJ, Siewers, IJ, Steffens, JJ & Benkovic, S 1974, 'Anomeric specificity of phosphofructokinase from rabbit muscle', Journal of Biological Chemistry, vol. 249, no. 19, pp. 6047-6051.

Anomeric specificity of phosphofructokinase from rabbit muscle. / Fishbein, R.; Benkovic, P. A.; Schray, K. J.; Siewers, I. J.; Steffens, J. J.; Benkovic, Stephen.

In: Journal of Biological Chemistry, Vol. 249, No. 19, 1974, p. 6047-6051.

Research output: Contribution to journalArticle

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T1 - Anomeric specificity of phosphofructokinase from rabbit muscle

AU - Fishbein, R.

AU - Benkovic, P. A.

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AU - Steffens, J. J.

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N2 - 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.

AB - 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.

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Fishbein R, Benkovic PA, Schray KJ, Siewers IJ, Steffens JJ, Benkovic S. Anomeric specificity of phosphofructokinase from rabbit muscle. Journal of Biological Chemistry. 1974;249(19):6047-6051.