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

John Chirgwin, E. A. Noltmann

Research output: Contribution to journalArticle

48 Citations (Scopus)

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 - 1975
Externally publishedYes

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Glucose-6-Phosphate Isomerase
Enzyme Inhibitors
Alkalinity
Anions
Phosphates
Acids
Enzymes
arabinonate-5-phosphate
6-phosphogluconic acid
4-phosphoerythronate

ASJC Scopus subject areas

  • Biochemistry

Cite this

The enediolate analogue 5 phosphoarabinonate as a mechanistic probe for phosphoglucose isomerase. / Chirgwin, John; Noltmann, E. A.

In: Journal of Biological Chemistry, Vol. 250, No. 18, 1975, p. 7272-7276.

Research output: Contribution to journalArticle

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