The enediolate analogue 5 phosphoarabinonate as a mechanistic probe for phosphoglucose isomerase

J. M. Chirgwin, E. A. Noltmann

Research output: Contribution to journalArticlepeer-review

49 Scopus citations

Abstract

A stable analogue has been prepared of the enediolate anion believed to occur transiently in the reaction of phosphoglucose isomerase. This compound, 5 phosphoarabinonate, is the strongest known competitive inhibitor of the enzyme (K(i) = 3 x 10-7M below pH 7). A distinctive pH dependence of binding, also found for two other aldonic acid ω phosphates, 6 phosphogluconate and 4 phosphoerythronate, involves perturbation of a pKa from 7.0 in the free enzyme to 9.0 in the enzyme inhibitor complex. This perturbation may reflect a catalytically advantageous increase in basicity which occurs around the transition state of the normal enzymatic reaction.

Original languageEnglish (US)
Pages (from-to)7272-7276
Number of pages5
JournalJournal of Biological Chemistry
Volume250
Issue number18
StatePublished - Dec 1 1975
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'The enediolate analogue 5 phosphoarabinonate as a mechanistic probe for phosphoglucose isomerase'. Together they form a unique fingerprint.

Cite this