Malic enzyme family: structural-biochemical analysis to improves catalytic properties

ALVAREZ, C. E.; SAIGO, M.; MUSSI, A.; GERRARD WHEELER, M. C.; ARIAS, C. L.; MAURINO, V. G.; DRINCOVICH, M. F.

Evento virtual

Congreso; LVII Reunión Anual SAIB ? XVI Reunión Anual SAMIGE; 2021

SAIB - SAMIGE

Structure-function studies contribute to deciphering how small modifications in the primary structure could introduce desirable characteristics into enzymes without affecting its overall functioning. Malic enzymes (ME) are ubiquitous and participate in different biological functions as diverse as lipogenesis, photosynthesis and organic acid metabolism. In the presence of a divalent cation, this enzyme catalyzes the oxidative decarboxylation of malate to pyruvate, NAD(P)H, and CO2. MEs of several sources including humans, pigeons, nematodes, bacteria, phytopathogens and plants have been kinetically and structurally characterized. Our results, which combine structural, biochemical, phylogenetic and functional analysis, show that this family has members with: different structural conformation (like homo/hetero-dimers, tetramers, bifunctional enzymes), post-translational modifications and species- or isoform-specific regulation. In relation to this, we recently gained novel information provided by the crystal structural analysis of the photosynthetic ME of maize and sorghum, and of the minimal functional ME structure known until now, from Candidatus Phytoplasma mali. Currently, we started applying all the knowledge obtained to perform rational design modification of two groups of enzymes: i. the bifunctional ME, which have high potential to produce new generation of biofertilizers; and ii. the photosynthetic ME, that is a key candidate to improve photosynthetic efficiency and crop yields. By these strategies, we try to develop new agronomic technologies for crops that has not reached their maximum potential and will not be enough to feed the world´s population in the near future.