Liu Tao, Zhu Ping, Cheng Ke-di, Meng Chao, Zhu Hui-xin
Institute of Materia Medica, Chinese Academy of Medical Sciences and Peking Union Medical College, #1 Xian Nong Tan Street, Beijing 100050, P. R. China.
Planta Med. 2005 Oct;71(10):987-9. doi: 10.1055/s-2005-871260.
A full-length cDNA encoding putrescine N-methyltransferase (PMT) was isolated from the hairy roots of A. tanguticus. Nucleotide sequence analysis of the cloned cDNA revealed an open reading frame of 1017 bp encoding 338 amino acids with high homology to other known PMTs. A. tanguticus PMT was expressed in Escherichia coli. The recombinant AtPMT was purified and exhibited S-adenosyl-methionine-dependent N-methyltransferase activity.
从唐古特青兰的毛状根中分离出了一个编码腐胺N-甲基转移酶(PMT)的全长cDNA。对克隆的cDNA进行核苷酸序列分析,发现一个1017 bp的开放阅读框,编码338个氨基酸,与其他已知的PMT具有高度同源性。唐古特青兰PMT在大肠杆菌中表达。重组AtPMT被纯化,并表现出依赖S-腺苷甲硫氨酸的N-甲基转移酶活性。