RT Journal Article
T1 Enzymes involved in the biosynthesis of arginine from ornithine in maritime pine (Pinus pinaster Ait.)
A1 Urbano-Gámez, Jose Alberto
A1 El-Azaz-Ciudad, Jorge
A1 Ávila-Sáez, Concepción
A1 De-la-Torre-Fazio, Fernando Nicolás
A1 Cánovas-Ramos, Francisco Miguel
K1 Biosíntesis
K1 Pinos - Metabolismo
AB 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 (Pinus pinaster Ait.) were produced in Escherichia coli 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.
PB MDPI
SN 2223-7747
YR 2020
FD 2020
LK https://hdl.handle.net/10630/37921
UL https://hdl.handle.net/10630/37921
LA eng
NO Urbano-Gámez, J.A.; El-Azaz, J.; Ávila, C.; de la Torre, F.N.; Cánovas, F.M. Enzymes Involved in the Biosynthesis of Arginine from Ornithine in Maritime Pine (Pinus pinaster Ait.). Plants 2020, 9, 1271. https://doi.org/10.3390/plants9101271
DS RIUMA. Repositorio Institucional de la Universidad de Málaga
RD 19 ene 2026