Maize recombinant non-C4 NADP-malic enzyme: A novel dimeric malic enzyme with high specific activity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2004-05

AUTHORS

Saigo Mariana, P. bologna Federico, G. maurino Verónica, Detarsio Enrique, S. andreo Carlos, F. drincovich María

ABSTRACT

Among the different isoforms of NADP-malic enzyme (NADP-ME) involved in a wide range of metabolic pathways in plants, the NADP-ME that participates in C4-photosynthesis is the most studied. In the present work, the expression in E. coli of a cDNA encoding for a maize non-photosynthetic NADP-ME is presented. The recombinant NADP-ME thus obtained presents kinetic and structural properties different from the enzyme previously purified from etiolated leaves and roots. Moreover, the recombinant non-photosynthetic NADP-ME presents very high intrinsic NADP-ME activity, which is unexpected for a non-C4 NADP-ME. Using antibodies against this recombinant enzyme, an immunoreactive band of 66 kDa is detected in different maize tissues indicating that the 66 kDa-NADP-ME is in fact a protein expressed in␣vivo. The recombinant NADP-ME assembles as a dimer, although the results obtained indicate that a higher molecular mass oligomeric state of the enzyme is found in maize roots in vivo. In this way, maize presents at least three NADP-ME isoforms: a 72 kDa constitutive form (previously characterized); the novel non-photosynthetic 66 kDa isoform characterized in this work (which is the product of the ZmChlMe2gene and the likely precursor to the evolution of the photosynthetic C4 NADP-ME) and the 62 kDa isoform (implicated in C4 photosynthesis). The contribution of the present work anticipates further studies concerning the equilibrium between the oligomeric states of the NADP-ME isoforms and the evolution towards the C4 isoenzyme in maize. More... »

PAGES

97-107

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s11103-004-0472-z

DOI

http://dx.doi.org/10.1007/s11103-004-0472-z

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1025393897

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/15604667


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