2024-12-162024-12-162023-02Torresi, Florencia; Rodriguez, Fernanda Mariana; Gomez Casati, Diego Fabian; Martín, Mariana; Two phosphoenolpyruvate carboxykinases with differing biochemical properties in Chlamydomonas reinhardtii; Elsevier Science; FEBS Letters; 597; 4; 2-2023; 585-5970014-5793https://hdl.handle.net/2133/28453Phosphoenolpyruvate carboxykinase (PEPCK) catalyses the reversible reac-tion of decarboxylation and phosphorylation of oxaloacetate (OAA) to gener-ate phosphoenolpyruvate (PEP) and CO2 playing mainly a gluconeogenic rolein green algae. We found two PEPCK isoforms in Chlamydomonas rein-hardtii and we cloned, purified and characterised both enzymes. Chlre-PEPCK1 is more active as decarboxylase than ChlrePEPCK2.ChlrePEPCK1 is hexameric and its activity is affected by citrate, phenylala-nine and malate, while ChlrePEPCK2 is monomeric and it is regulated bycitrate, phenylalanine and glutamine. We postulate that the two PEPCK iso-forms found originate from alternative splicing of the gene or regulated prote-olysis of the enzyme. The presence of these two isoforms would be part of amechanism to finely regulate the biological activity of PEPCKs.585–597enopenAccessAlgal pepckChlamydomonas reinhardtiiPhosphoenolpyruvate carboxykinasePepckarticuloFederation of European Biochemical SocietiesUniversidad Nacional de RosarioAttribution-NonCommercial-NoDerivatives 4.0 International