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|標題:||Interactions between coenzyme B(12) analogs and adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum||作者:||Chen, H.P.
|關鍵字:||adenosylcobalamin;adenosylcobinamide;AdoCbi-GDP;B(12);glutamate;mutase;salmonella-typhimurium lt2;methylmalonyl-coa mutase;guanylyltransferase cobu;heterologous expression;fusion protein;purification;enzyme;adenosylcobinamide;catalysis;binding||Project:||Febs Journal||期刊/報告no：:||Febs Journal, Volume 275, Issue 23, Page(s) 5960-5968.||摘要:||
Adenosylcobalamin (AdoCbl)-dependent glutamate mutase from Clostridium tetanomorphum comprises two weakly-associating subunits, MutS and MutE, which combine with AdoCbl to form the active holo-enzyme. Three coenzyme analogs, methylcobinamide (MeCbi), adenosylcobinamide (AdoCbi) and adeosylcobinamide-GDP (AdoCbi-GDP), were synthesized at milligram scale. Equilibrium dialysis was used to measure the binding of coenzyme B(12) analogs to glutamate mutase. Our results show that, unlike AdoCbl-dependent methylmalonyl CoA mutase, the ratio k(cat)/K(m) decreased approximately 10(4)-fold in both cases when AdoCbi or AdoCbi-GDP was used as the cofactor. The coenzyme analog-binding studies show that, in the absence of the ribonucleotide tail of AdoCbl, the enzyme's active site cannot correctly accommodate the coenzyme analog AdoCbi. The results presented here shed some light on the cobalt-carbon cleavage mechanism of B(12).
|Appears in Collections:||分子生物學研究所|
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