Open AccessPhosphoenolpyruvate carboxykinase in cherry (Prunus avium L.) fruit during development
Author(s) -
Robert P. Walker,
Alberto Battistelli,
Stefano Moscatello,
Z.-H. Chen,
R. C. Leegood,
Franco Famiani
Publication year - 2011
Publication title -
journal of experimental botany
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.616
H-Index - 242
eISSN - 1460-2431
pISSN - 0022-0957
DOI - 10.1093/jxb/err189
Subject(s) - phosphoenolpyruvate carboxylase , phosphoenolpyruvate carboxykinase , pyruvate carboxylase , gluconeogenesis , flesh , biochemistry , prunus armeniaca , prunus , malic acid , biology , carboxy lyases , enzyme , rubisco , malic enzyme , chemistry , botany , horticulture , cultivar , citric acid , dehydrogenase
In this study the abundance and location of phosphoenolpyruvate carboxykinase (PEPCK) was determined in the flesh and skin of the sweet cherry (Prunus avium L.) cultivar Durone Nero II during development. PEPCK was not present in young fruit but appeared in both tissues as the fruit increased in size. In these there was no net dissimilation of malic acid, which accounts for the bulk of their organic acid contents when PEPCK was present. To assist in understanding the function of PEPCK, the abundance of a number of other enzymes was determined. These enzymes were aspartate aminotransferase (AspAT), glutamine synthetase (GS), phosphoenolpyruvate carboxylase (PEPC), pyruvate, orthophosphate dikinase (PPDK), and ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco). A potential role for PEPCK in the regulation of pH and the utilization of malate in gluconeogenesis in the flesh and skin of cherries is presented.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom