Structure and mechanism of spermidine synthases
Structure and mechanism of spermidine synthases
复制标题
DOI：
10.1021/bi602498k
复制
发表时间：
2007-07-17
期刊：
影响因子：
2.9
通讯作者：
Plotnikov, Alexander N.
中科院分区：
文献类型：
--
作者：
Wu, Hong;Min, Jinrong;Plotnikov, Alexander N.
氨丙基转移酶将氨丙基从脱羧的S-腺苷甲硫氨酸转移到胺受体，形成多胺。结构和生物化学研究已经进行了与人类亚精胺合酶，这是高度特异性的腐胺作为胺受体，和Thermotoga maritima亚精胺合酶，它更喜欢腐胺，但更宽容的其他基板。比较了人精脒合酶的底物和产物与T.与多底物类似物抑制剂复合的maritima亚精胺合酶和定点突变体性质的分析提供了氨丙基转移反应的一般机理假说。这些研究也为氨丙基转移酶家族亚精胺合酶亚类的特异性提供了结构基础。
Aminopropyltransferases transfer aminopropyl groups from decarboxylated S-adenosylmethionine to amine acceptors, forming polyamines. Structural and biochemical studies have been carried out with the human spermidine synthase, which is highly specific for putrescine as the amine acceptor, and the Thermotoga maritima spermidine synthase, which prefers putrescine but is more tolerant of other substrates. Comparison of the structures of the human spermidine synthase with both substrates and products with the known structure of T. maritima spermidine synthase complexed to a multisubstrate analogue inhibitor and analysis of the properties of site-directed mutants provide a general mechanistic hypothesis for the aminopropyl transfer reaction. The studies also provide a structural basis for the specificity of the spermidine synthase subclass of the aminopropyltransferase family.