Bukin Iu V, Sergeev A B, Florent'ev V L
Biokhimiia. 1976 Apr;41(4):614-8.
It is shown in the system with partially purified pyridoxal kinase from mouse liver, that the presence of one alkyl group in the 2nd or 6th positions of pyridine cycle in pyridoxole and pyridoxamine derivatives and pyridoxal oximes is a necessary condition which determines relatively high affinity of structural vitamin B6 analogues to the enzyme. 2'-n-Propylpyridoxal was phosphorylated by pyridoxal kinase with a relatively high rate, while 2-nor-6-methylpyridoxal, having a similar affinity to pyridoxal kinase, was not phosphorylated at all. The data obtained indicate an important role of the methyl group in the 2nd position of pyridine cycle in vitamin B6 molecule for its fixation in the enzyme active site and for the proper orientation, which provides enzymatic substrate phosphorylation. Some structural peculiarities of vitamin B6 analogues are considered, pre-determining their low or high efficiency as vitamin B6 antimetabolite in vivo.
在含有部分纯化的小鼠肝脏吡哆醛激酶的系统中表明，吡哆醇和吡哆胺衍生物以及吡哆醛肟的吡啶环第2位或第6位存在一个烷基，是决定结构型维生素B6类似物对该酶具有较高亲和力的必要条件。2'-正丙基吡哆醛被吡哆醛激酶磷酸化的速率相对较高，而与吡哆醛激酶具有相似亲和力的2-去甲-6-甲基吡哆醛则完全不被磷酸化。所获得的数据表明，维生素B6分子吡啶环第2位的甲基对于其在酶活性位点的固定以及提供酶促底物磷酸化的正确取向具有重要作用。还考虑了维生素B6类似物的一些结构特点，这些特点决定了它们在体内作为维生素B6抗代谢物的低效率或高效率。
