Progress in Establishing the Rate-Limiting Features and Kinetic Mechanism of the Glyceraldehyde-3-phosphate Dehydrogenase Reaction

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Abstract

Primary hydrogen isotope effects and steady-state kinetics have been used to study the mechanism of glyceraldehyde-3-phosphate (GAP) dehydrogenase at pH 8.6. The isotope effect determined by using GAP-Id was unity and independent of arsenate (used as the acyl acceptor) and NAD+ concentrations when the aldehyde substrate was at saturating concentrations. At low GAP concentrations (apparent V/K conditions), the primary hydrogen isotope effect (H/D) was in the range of 1.40-1.52 and independent of arsenate and NAD+ concentrations. Apparent V/K for NAD+ was independent of GAP concentration, and apparent V/K for GAP was independent of NAD+ concentration. The dependence of apparent V/K for GAP on arsenate concentration was more complex but extrapolated to nonzero V/K at the zero-arsenate intercept. These observations are consistent with the general features of the Segal and Boyer (1953) mechanism for the reaction.

Original languageEnglish (US)
Pages (from-to)6898-6903
Number of pages6
JournalBiochemistry
Volume31
Issue number30
DOIs
StatePublished - Feb 1 1992

All Science Journal Classification (ASJC) codes

  • Biochemistry

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