The covalent binding of d-fructose 1,6-diphosphate to muscle aldolase
1972; Elsevier BV; Volume: 153; Issue: 1 Linguagem: Inglês
10.1016/0003-9861(72)90454-7
ISSN1096-0384
Autores Tópico(s)Amino Acid Enzymes and Metabolism
ResumoRabbit muscle aldolase was reduced with sodium borohydride (or cyanoborohydride) in the presence of specifically labeled [3H]- and [14C]fructose 1,6-diphosphate. Under steady-state conditions, about 10–15% of the specific ϵ-lysine catalytic sites were bound to fructose 1,6-diphosphate by a covalent ketimine linkage. The remaining substituted lysine residues were identified as N6-β-glyceryllysine. The results argue against a concerted mechanism of binding and cleavage of fructose 1,6-diphosphate by type I aldolases.
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