Mamaeva O K, Karpeĭskiĭ M Ia, Karpeĭskiĭ A M, Bibilashvili R Sh
Mol Biol (Mosk). 1979 Jul-Aug;13(4):811-21.
The interaction of pyridoxal, pyridoxal-5'-mono-, di- and triphosphate with certain enzymes of polynucleotide synthesis (DNA-dependent RNA polymerase, DNA-dependent DNA polymerase I and polynucleotide phosphorylase from Escherichia coli and terminal deoxyribonucleotide transferase from calf thymus) was studied. All compounds tested was found to be reversible and competitive inhibitors of these enzymes. The reduction of the enzyme-inhibitor complex with NaBH4 gives rise to the complete irreversible inhibition of the enzymes under study. The comparison of the inhibition constants for pyridoxal and its phosphorylated derivatives with those for mono-, di- and triphosphates of nucleosides was carried out for the enzymes. The results obtained suggest that the modified epsilon-amino-group of lysine residue should be localized at the catalytic site in the vicinity of the pyrophosphate binding area of an enzyme.
研究了吡哆醛、吡哆醛-5'-单磷酸、二磷酸和三磷酸与多核苷酸合成的某些酶（大肠杆菌的依赖DNA的RNA聚合酶、依赖DNA的DNA聚合酶I和多核苷酸磷酸化酶以及小牛胸腺的末端脱氧核糖核苷酸转移酶）之间的相互作用。发现所有测试的化合物都是这些酶的可逆竞争性抑制剂。用NaBH4还原酶-抑制剂复合物会导致所研究的酶完全不可逆抑制。对这些酶比较了吡哆醛及其磷酸化衍生物与核苷单磷酸、二磷酸和三磷酸的抑制常数。所得结果表明，赖氨酸残基的修饰ε-氨基应位于酶焦磷酸结合区域附近的催化位点。
