Haines Ricci J, Pendleton Laura C, Eichler Duane C
Department of Molecular Medicine, University of South Florida, College of Medicine, 12901 Bruce B. Downs Blvd., MDC Box 7, Tampa, Florida 33612, USA.
Int J Biochem Mol Biol. 2011;2(1):8-23.
The levels of L-arginine, a cationic, semi-essential amino acid, are often controlled within a cell at the level of local availability through biosynthesis. The importance of this temporal and spatial control of cellular L-arginine is highlighted by the tissue specific roles of argininosuccinate synthase (argininosuccinate synthetase) (EC 6.3.4.5), as the rate-limiting step in the conversion of L-citrulline to L-arginine. Since its discovery, the function of argininosuccinate synthase has been linked almost exclusively to hepatic urea production despite the fact that alternative pathways involving argininosuccinate synthase were defined, such as its role in providing arginine for creatine and for polyamine biosynthesis. However, it was the discovery of nitric oxide that meaningfully extended our understanding of the metabolic importance of non-hepatic argininosuccinate synthase. Indeed, our knowledge of the number of tissues that manage distinct pools of arginine under the control of argininosuccinate synthase has expanded significantly.
L-精氨酸是一种阳离子半必需氨基酸,其水平通常在细胞内通过生物合成在局部可用性水平上受到控制。精氨琥珀酸合酶(精氨琥珀酸合成酶)(EC 6.3.4.5)在组织中的特定作用突出了细胞内L-精氨酸这种时空控制的重要性,它是L-瓜氨酸转化为L-精氨酸过程中的限速步骤。自发现以来,尽管已经确定了涉及精氨琥珀酸合酶的替代途径,例如其在为肌酸和多胺生物合成提供精氨酸方面的作用,但精氨琥珀酸合酶的功能几乎一直仅与肝脏尿素生成相关。然而,一氧化氮的发现有意义地扩展了我们对非肝脏精氨琥珀酸合酶代谢重要性的理解。事实上,我们对在精氨琥珀酸合酶控制下管理不同精氨酸池的组织数量的认识有了显著扩展。