Artigo Revisado por pares

Irreversible inactivation of triose phosphate isomerase by 1-hydroxy-3-iodo-2-propanone phosphate

1968; Elsevier BV; Volume: 33; Issue: 6 Linguagem: Inglês

10.1016/0006-291x(68)90395-1

ISSN

1090-2104

Autores

F.C. Hartman,

Tópico(s)

Diet, Metabolism, and Disease

Resumo

I have synthesized 1-hydroxy-3-iodo-2-propanone phosphate, a compound structurally similar to dihydroxyacetone phosphate, as a potential active-site specific reagent for triose phosphate isomerase. Under mild conditions, the reagent irreversibly inactivates the enzyme. The kinetics of the inactivation in the absence or presence of the competitive inhibitor α-glycerophosphate, the stoichimetric incorporation of the reagent, and the similarities of the pH dependencies of enzymic activity and of the inactivation rate are indicative of a specific modification at the active site of triose phosphate isomerase.

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