Iakusheva M I, Poznanskaia A A, Pospelova T A, Rudakova I P, Iurkevich A M
Biokhimiia. 1977 Nov;42(11):2086-8.
The behavior of two coenzyme analogs, [(5-aden-9-yl)methoxyethyl] cob (III) alamin and [(5-aden-9-yl)pentyl] cob (III) alamin modified at the nucleoside ligand sugar moiety was studied in the system of adenosyl-cobalamin-dependent glycerol dehydratase from Aerobacter aerogenes. It was shown that neither of the analogs possesses coenzyme properties and that both are strong competitive inhibitors for adenosylcobalamin (AdoCbl). The affinity of the two analogs for the apoenzyme is higher than that of AdoCbl. The data obtained are indicative of the essential role of the ribofuranoside fragment of AdoCbl in the manifestation of the coenzyme activity. The apoenzyme interaction with the analogs under study is discussed in terms of the Dreiding stereomodels for AdoCbl and its analogs.
在产气气杆菌的腺苷钴胺素依赖性甘油脱水酶体系中，研究了两种在核苷配体糖部分修饰的辅酶类似物，即[(5-腺苷-9-基)甲氧基乙基]钴胺(III)和[(5-腺苷-9-基)戊基]钴胺(III)的行为。结果表明，这两种类似物均不具有辅酶性质，且都是腺苷钴胺素（AdoCbl）的强竞争性抑制剂。这两种类似物对脱辅基酶的亲和力高于AdoCbl。所获得的数据表明，AdoCbl的呋喃核糖苷片段在辅酶活性的表现中起重要作用。根据AdoCbl及其类似物的德雷丁立体模型，讨论了脱辅基酶与所研究类似物的相互作用。
