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参与海岸松(Ait.)中从鸟氨酸生物合成精氨酸的酶。

Enzymes Involved in the Biosynthesis of Arginine from Ornithine in Maritime Pine ( Ait.).

作者信息

Urbano-Gámez José Alberto, El-Azaz Jorge, Ávila Concepción, de la Torre Fernando N, Cánovas Francisco M

机构信息

Grupo de Biología Molecular y Biotecnología, Departamento de Biología Molecular y Bioquímica, Universidad de Málaga, Campus Universitario de Teatinos, 29071 Málaga, Spain.

出版信息

Plants (Basel). 2020 Sep 27;9(10):1271. doi: 10.3390/plants9101271.

Abstract

The amino acids arginine and ornithine are the precursors of a wide range of nitrogenous compounds in all living organisms. The metabolic conversion of ornithine into arginine is catalyzed by the sequential activities of the enzymes ornithine transcarbamylase (OTC), argininosuccinate synthetase (ASSY) and argininosuccinate lyase (ASL). Because of their roles in the urea cycle, these enzymes have been purified and extensively studied in a variety of animal models. However, the available information about their molecular characteristics, kinetic and regulatory properties is relatively limited in plants. In conifers, arginine plays a crucial role as a main constituent of N-rich storage proteins in seeds and serves as the main source of nitrogen for the germinating embryo. In this work, recombinant PpOTC, PpASSY and PpASL enzymes from maritime pine ( Ait.) were produced in to enable study of their molecular and kinetics properties. The results reported here provide a molecular basis for the regulation of arginine and ornithine metabolism at the enzymatic level, suggesting that the reaction catalyzed by OTC is a regulatory target in the homeostasis of ornithine pools that can be either used for the biosynthesis of arginine in plastids or other nitrogenous compounds in the cytosol.

摘要

在所有生物中,氨基酸精氨酸和鸟氨酸是多种含氮化合物的前体。鸟氨酸向精氨酸的代谢转化由鸟氨酸转氨甲酰酶(OTC)、精氨琥珀酸合成酶(ASSY)和精氨琥珀酸裂解酶(ASL)的顺序活性催化。由于它们在尿素循环中的作用,这些酶已在多种动物模型中得到纯化和广泛研究。然而,关于它们的分子特征、动力学和调节特性的现有信息在植物中相对有限。在针叶树中,精氨酸作为种子中富含氮的储存蛋白的主要成分发挥着关键作用,并作为萌发胚的主要氮源。在这项工作中,来自海岸松(Ait.)的重组PpOTC、PpASSY和PpASL酶在(此处原文缺失具体表达)中产生,以便研究它们的分子和动力学特性。这里报道的结果为在酶水平上调节精氨酸和鸟氨酸代谢提供了分子基础,表明OTC催化的反应是鸟氨酸池稳态中的一个调节靶点,鸟氨酸池可用于质体中精氨酸的生物合成或细胞质中其他含氮化合物的合成。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/82a7/7601404/0228f2dc3efe/plants-09-01271-g001.jpg

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