Hartmeier G M, Sawhney A K, Yang B I
Biochem Biophys Res Commun. 1983 Apr 29;112(2):629-37. doi: 10.1016/0006-291x(83)91510-3.
Forty compounds were surveyed for their effect on the activation of pig heart apoaspartate aminotransferase by pyridoxamine 5'-phosphate. Most of the nucleotides, sugar phosphates, coenzymes, phospholipid precursors and inorganic oxyanions tested were found to be inhibitory. With few exceptions, the only requirement for a substance to be inhibitory is the presence of a di- or polyanionic moiety analogous to the 5'-phosphate group of the cofactor. In spite of the lack of overall structural similarity to pyridoxamine 5'-phosphate, inorganic pyrophospate and apparently other inhibitors are characterized by dissociation constants comparable in magnitude to that previously reported for the natural cofactor. The physiological significance of the inhibition of coenzyme activation of apoaspartate aminotransferase by these common biological compounds is not known.
检测了40种化合物对磷酸吡哆胺激活猪心脏脱辅基天冬氨酸转氨酶的影响。结果发现，所测试的大多数核苷酸、糖磷酸酯、辅酶、磷脂前体和无机氧阴离子均具有抑制作用。除少数例外，一种物质具有抑制作用的唯一条件是存在与辅因子5'-磷酸基团类似的二价或多价阴离子部分。尽管无机焦磷酸和其他一些抑制剂与磷酸吡哆胺在整体结构上缺乏相似性，但其解离常数的大小与先前报道的天然辅因子相当。这些常见生物化合物对脱辅基天冬氨酸转氨酶辅酶激活的抑制作用的生理意义尚不清楚。
