Slow reversible inhibitions of rabbit muscle aldolase with substrate analogues: synthesis, enzymatic kinetics and UV difference spectroscopy studies.

Abstract:

:Various dihydroxyacetone-phosphate (DHAP) analogues bearing an aromatic ring or beta-dicarbonyl structures were synthesized. Their capacity to form a stabilized iminium ion or conjugated enamine in the reaction catalyzed by rabbit muscle aldolase (EC 4.1.2.13) were investigated by enzymatic kinetics and UV difference spectroscopic techniques. Whereas the aromatic derivative led to competitive inhibition without detectable iminium ion formation, slow reversible inhibitions of aldolase by beta-dicarbonyl compounds was shown to have taken place. Conjugated enamine formation at the active site of the enzyme was detected by their specific absorbances close to 317 nm.

journal_name

Bioorg Med Chem

authors

Gefflaut T,Blonski C,Périé J

doi

10.1016/s0968-0896(96)00221-0

subject

Has Abstract

pub_date

1996-12-01 00:00:00

pages

2043-54

issue

12

eissn

0968-0896

issn

1464-3391

pii

S0968-0896(96)00221-0

journal_volume

4

pub_type

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