The human arginases and arginase deficiency
The human arginases and arginase deficiency
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DOI：
10.1023/a:1005313809037
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发表时间：
1998-06-01
影响因子：
4.2
通讯作者：
Cederbaum, S
中科院分区：
文献类型：
--
作者：
Iyer, R;Jenkinson, CP;Cederbaum, S
精氨酸酶是尿素循环中的最终酶。它的缺陷是该周期中最不常被描述的疾病。它主要导致血液精氨酸升高，较少导致血氨持续或急性升高。这似乎是由于主要在肾脏中表达的第二个精氨酸酶位点所致，可以招募该位点来部分补偿肝脏精氨酸酶的缺乏。肝脏精氨酸酶基因结构允许对患有该疾病的患者进行分子病理学研究，并且提出了这些研究的结果以及关于蛋白质结构的推论。所有精氨酸酶中的保守区域允许克隆 AII（第二种精氨酸酶亚型）。它已定位于线粒体，并被认为参与鸟氨酸生物合成。它具有主要保守的蛋白质序列，肝精氨酸酶基因的结构特征也保守。当比较不同物种的 AI 和 AII 时，两者似乎在两栖动物进化之前的某个时间就出现了分歧。提出了 AII 在一氧化氮和多胺代谢中的作用的证据，这似乎与组织分布的数据一致。
Arginase is the final enzyme in the urea cycle. Its deficiency is the least frequently described disorder of this cycle. It results primarily in elevated blood arginine, and less frequently in either persistent or acute elevations in blood ammonia. This appears to be due to a second arginase locus, expressed primarily in the kidney, which can be recruited to compensate, in part, for the deficiency of liver arginase. The liver arginase gene structure permitted study of the molecular pathology of patients with the disorder and the results of these studies and the inferences about the protein structure are presented. The conserved regions among all arginases allowed the cloning of AII, the second arginase isoform. It has been localized to the mitochondrion and is thought to be involved in ornithine biosynthesis. It shares the major conserved protein sequences, and structural features of liver arginase gene are also conserved. When AI and AII from various species are compared, it appears that the two diverged some time prior to the evolution of amphibians. The evidence for the role of AII in nitric oxide and polyamine metabolism is presented and this appears consonant with the data on the tissue distribution.