Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus
Cloning of human agmatinase. An alternate path for polyamine synthesis induced in liver by hepatitis B virus
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DOI：
10.1152/ajpgi.00386.2001
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发表时间：
2002-02-01
影响因子：
4.5
通讯作者：
Morris, SM
中科院分区：
文献类型：
--
作者：
Mistry, SK;Burwell, TJ;Morris, SM
胍丁胺酶将胍丁胺水解为腐胺和尿素，不仅代表了调节哺乳动物细胞中胍丁胺生物效应的潜在重要机制，而且代表了用于多胺生物合成的鸟氨酸脱羧酶的替代品。我们已经分离出编码人胍丁胺酶的全长cDNA，其功能通过酵母中的互补得到证实。位于 1 号染色体上的单拷贝人类胍丁胺酶基因编码一种 352 个残基的蛋白质，在 NH3 末端具有假定的线粒体靶向序列。人凝胺酶与细菌凝胺酶有约 30% 的同一性
Agmatinase, which hydrolyzes agmatine to putrescine and urea, not only represents a potentially important mechanism for regulating the biological effects of agmatine in mammalian cells but also represents an alternative to ornithine decarboxylase for polyamine biosynthesis. We have isolated a full-length cDNA encoding human agmatinase whose function was confirmed by complementation in yeast. The single-copy human agmatinase gene located on chromosome 1 encodes a 352-residue protein with a putative mitochondrial targeting sequence at the NH3-terminus. Human agmatinase has about 30% identity to bacterial agmatinases and