The anomeric form of D fructose 1,6 biphosphate used as substrate in the muscle and yeast aldolase reactions

K. J. Schray, R. Fishbein, W. P. Bullard, S. J. Benkovic

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

From a series of rapid quench kinetic experiments, it has been demonstrated that muscle D fructose bisphosphate aldolase catalyzes the cleavage of β D fructose 1,6 bisphosphate but not that of the α anomer, although the α anomer may be tightly bound. Yeast D fructose bisphosphate aldolase appears to utilize both α and β anomers of the substrate, with yeast apoaldolase catalyzing the interconversion of the α and β forms.

Original languageEnglish (US)
Pages (from-to)4883-4887
Number of pages5
JournalJournal of Biological Chemistry
Volume250
Issue number13
StatePublished - Dec 1 1975

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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