Effects of chirality and substituents at carbon 3 in dihydroxyacetone-phosphate analogues on their binding to rabbit muscle aldolase

C Blonski; T Gefflaut; J Perie

doi:10.1016/0968-0896(95)00093-v

Effects of chirality and substituents at carbon 3 in dihydroxyacetone-phosphate analogues on their binding to rabbit muscle aldolase

Bioorg Med Chem. 1995 Sep;3(9):1247-53. doi: 10.1016/0968-0896(95)00093-v.

Authors

C Blonski¹, T Gefflaut, J Perie

Affiliation

¹ Groupe de Chimie Organique Biologique, URA au CNRS 470, Université Paul Sabatier, Toulouse, France.

PMID: 8564417
DOI: 10.1016/0968-0896(95)00093-v

Abstract

A series of dihydroxyacetone-phosphate (DHAP) analogues has been synthesized, differing in their stereochemistry and functionality at C-3. The kinetic effects of these compounds on the enzyme aldolase (EC 4.1.2.13) have been studied and differing modes of action observed. Competitive and time dependent reversible inhibition have been shown to take place both with and without borohydride detected formation of an immonium ion.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Binding Sites
Binding, Competitive
Dihydroxyacetone Phosphate / analogs & derivatives*
Dihydroxyacetone Phosphate / chemical synthesis
Dihydroxyacetone Phosphate / metabolism*
Enzyme Inhibitors / chemical synthesis*
Enzyme Inhibitors / metabolism*
Enzyme Inhibitors / pharmacology
Fructose-Bisphosphate Aldolase / antagonists & inhibitors
Fructose-Bisphosphate Aldolase / metabolism*
Kinetics
Muscles / enzymology*
Organophosphates / metabolism
Organophosphates / pharmacology
Propylene Glycols / metabolism
Propylene Glycols / pharmacology
Rabbits
Schiff Bases / metabolism
Stereoisomerism
Structure-Activity Relationship

Substances

Enzyme Inhibitors
Organophosphates
Propylene Glycols
Schiff Bases
3-hydroxypropane-1-phosphate
Dihydroxyacetone Phosphate
Fructose-Bisphosphate Aldolase