Evidence map›Paper›PMID 15604667›Full record

ArticlePlant molecular biology2004

Maize recombinant non-C4 NADP-malic enzyme: a novel dimeric malic enzyme with high specific activity.

Mariana Saigo, Federico P Bologna, Verónica G Maurino, Enrique Detarsio, Carlos S Andreo, María F Drincovich

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Article in Plant molecular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.7field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 56 citations in OpenAlex.

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  8. 2-Hydroxy Acids in Plant Metabolism.The arabidopsis book · 2015
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Mariana SaigoCentro de Estudios Fotosintéticos y Bioquímicos (CEFOBI), Universidad Nacional de Rosario, Suipacha 531, Argentina.
Federico P Bologna
Verónica G Maurino
Enrique Detarsio
Carlos S Andreo
María F Drincovich
National University of Rosario · ARCentro de Estudios Fotosintéticos y Bioquímicos · ARUniversity of Cologne · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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 C(4)-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-C( 4) 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 ZmChlMe2 gene and the likely precursor to the evolution of the photosynthetic C(4) NADP-ME) and the 62 kDa isoform (implicated in C(4) 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 C(4) isoenzyme in maize.

Indexed as

Amino Acid SequenceBlotting, WesternCloning, MolecularDimerizationDNA, ComplementaryGene Expression Regulation, EnzymologicGene Expression Regulation, PlantIsoenzymesKineticsMalate DehydrogenaseMolecular Sequence DataMolecular WeightRecombinant ProteinsReverse Transcriptase Polymerase Chain ReactionSequence AlignmentSequence Analysis, DNADNA, ComplementaryIsoenzymesMalate Dehydrogenasemalate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)Recombinant Proteins

Identifiers

PMID15604667
OpenAlexW2414854013

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.