Cloning and characterization of human agmatinase
Cloning and characterization of human agmatinase
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DOI：
10.1006/mgme.2001.3277
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发表时间：
2002-03-01
影响因子：
3.8
通讯作者：
Cederbaum, SD
中科院分区：
文献类型：
--
作者：
Iyer, RK;Kim, HK;Cederbaum, SD
精氨酸脱羧酶（ADC）和胍丁胺酶是大肠杆菌中操纵子的一部分，构成精氨酸合成多胺的主要途径。这种途径也已知存在于植物中，但直到最近，无论是胍丁胺还是ADC，合成它的酶，还是胍丁胺酶，负责将胍丁胺转化为腐胺的酶，都不知道存在于人类或其他哺乳动物中。我们在这里描述胍丁胺酶基因的克隆和其转录产物的组织分布。人胍丁胺酶含有352个氨基酸残基，计算分子量为37，688kDa。与E.大肠杆菌胍基丁胺酶和42%的相似性，以人类的胍基丁胺酶I和II和共享高度保守的底物结合域与这些良好的表征酶。(C)2002 Elsevier Science（美国）。
Arginine decarboxylase (ADC) and agmatinase are part of an operon in Escherichia coli, which constitutes the primary pathway of polyamine synthesis from arginine. This pathway is also known to exist in plants, but until recently, neither agmatine nor ADC, the enzyme that synthesizes it, nor agmatinase the enzyme that is responsible for conversion of agmatine to putrescine, were known to exist in man or other mammals. We describe here the cloning of the agmatinase gene and the tissue distribution of its transcription product. Human agmatinase contains 352 amino acid residues and has a calculated molecular weight of 37,688 kDa. It has 56% similarity to E. coli agmatinase and 42% similarity to human arginases I and II and shares highly conserved substrate-binding domains with these well-characterized enzymes. (C) 2002 Elsevier Science (USA).