Kinetic and spectroscopic study of slow-binding inhibition processes in aldolase
β Scribed by C. Blonski; T. Gefflaut; J. Perie
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 120 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0894-3230
No coin nor oath required. For personal study only.
β¦ Synopsis
Compounds similar in structure to reactants, intermediates and products of the aldolase-catalysed reaction were synthesized and their affinities for the enzyme determined. The best situations were found with bdicarbonyl phosphorylated compounds which are a good mimics of the incoming groups in the bond-forming process; the corresponding binding is characterized by slow-binding inhibition type, the inhibitors forming stabilized iminium ions and enamines with the enzyme; similar effects were obtained with an aromatic aldehyde, also capable of forming a stabilized iminium ion. The use of aldolase mutants allows one to characterize the lysyl group involved in the process and also to suggest a proton transfer mechanism for the iminium ion formation with the enzyme natural substrate.
π SIMILAR VOLUMES
Electrochemical processes in the mercury-solution interphase were probed by in situ spectroelectrochemical micro-Raman spectroscopy. This is the Γrst report of the in situ characterization of electrochemical processes for a pure mercury electrode by Raman spectroscopy. Mercury was oxidized in 0.1 M
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 wi
A novel method based on steady state Γuorescence (SSF) measurements is introduced for studying slow release and swelling processes in gels formed by free radical crosslinking copolymerization (FCC) of methyl methacrylate (MMA) and ethylene glycol dimethacrylate (EGDM) in toluene. Gels were prepared