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. 2023 Feb;597(4):585-597.
doi: 10.1002/1873-3468.14590. Epub 2023 Feb 7.

Two phosphoenolpyruvate carboxykinases with differing biochemical properties in Chlamydomonas reinhardtii

Florencia Torresi  1   2 , Fernanda M Rodriguez  2   3 , Diego F Gomez-Casati  1   2 , Mariana Martín  1   2
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Free article

Two phosphoenolpyruvate carboxykinases with differing biochemical properties in Chlamydomonas reinhardtii

Florencia Torresi et al. FEBS Lett. 2023 Feb.
Free article

Abstract

Phosphoenolpyruvate carboxykinase (PEPCK) catalyses the reversible reaction of decarboxylation and phosphorylation of oxaloacetate (OAA) to generate phosphoenolpyruvate (PEP) and CO2 playing mainly a gluconeogenic role in green algae. We found two PEPCK isoforms in Chlamydomonas reinhardtii and we cloned, purified and characterised both enzymes. ChlrePEPCK1 is more active as decarboxylase than ChlrePEPCK2. ChlrePEPCK1 is hexameric and its activity is affected by citrate, phenylalanine and malate, while ChlrePEPCK2 is monomeric and it is regulated by citrate, phenylalanine and glutamine. We postulate that the two PEPCK isoforms found originate from alternative splicing of the gene or regulated proteolysis of the enzyme. The presence of these two isoforms would be part of a mechanism to finely regulate the biological activity of PEPCKs.

Keywords: Chlamydomonas reinhardtii; PEPCK; algal PEPCK; phosphoenolpyruvate carboxykinase.

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References

    1. Utter MF and Kolenbrander HM (1972) Formation of oxalacetate by CO2 fixation on phosphoenolpyruvate. In The Enzymes (Boyer PD, ed.), pp. 117-168. Elsevier, Amsterdam.
    1. Leegood RC and Walker RP (2003) Regulation and roles of phosphoenolpyruvate carboxykinase in plants. Arch Biochem Biophys 414, 204-210.
    1. Rosewich UL and Kistler HC (2000) Role of horizontal gene transfer in the evolution of fungi. Annu Rev Phytopathol 38, 325-363.
    1. Chiba Y, Miyakawa T, Shimane Y, Takai K, Tanokura M and Nozaki T (2019) Structural comparisons of phosphoenolpyruvate carboxykinases reveal the evolutionary trajectories of these phosphodiester energy conversion enzymes. J Biol Chem 294, 19269-19278.
    1. Koendjbiharie JG, van Kranenburg R and Kengen SW (2021) The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism. FEMS Microbiol Rev 45, fuaa061.

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