Origin of the Slow-Binding Inhibition of Aldolase by D-glycero-Tetrulose 1-Phosphate (D-Erythrulose 1-Phosphate) from the Comparison with the Isosteric Phosphonate Analog
✍ Scribed by Patrick Page; Casimir Blonski; Jacques Périé
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 246 KB
- Volume
- 1999
- Category
- Article
- ISSN
- 1434-193X
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✦ Synopsis
The mechanistic reaction pathway for the slow-binding enamine intermediate. We show from these results that enzyme slow-binding inhibition by D-erythrulose 1-inhibition of rabbit muscle aldolase by D-glycero-tetrulose 1phosphate (D-erythrulose 1-phosphate) was investigated phosphate is consistent with a phosphate β-elimination reaction through the enamine intermediate. This mechanism through the use of its phosphonomethyl isoster 4 which was synthezised for this study. The latter is not a substrate nor a takes into account the stereochemical features known for aldolase, the parallel between enzyme activity recovery and slow-binding inhibitor but interferes in the enzymecatalyzed reaction with the substrate fructose 1,6-phosphate release after action of D-erythrulose 1-phosphate, and also the same reaction from dihydroxyacetone diphosphate in a competitive manner. It was found that phosphonate 4 forms an iminium ion with aldolase and phosphate. undergoes subsequent α-proton abstraction to form an