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Characterization ofJBURE-IIb isoform ofCanavalia ensiformis(L.) DC urease Fernanda MulinariArlete Beatriz Becker‐RittDiogo Ribeiro Demartini2011 год

Characterization of JBURE-IIb isoform of Canavalia ensiformis (L.) DC urease
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Аннотация: Ureases, nickel-dependent enzymes that catalyze the hydrolysis of urea into ammonia and bicarbonate, are widespread in plants, bacteria, and fungi. Previously, we cloned a cDNA encoding a Canavalia ensiformis urease isoform named JBURE-II, corresponding to a putative smaller urease protein (78kDa) when compared to other plant ureases. Aiming to produce the recombinant protein, we obtained jbure-IIb, with different 3' and 5' ends, encoding a 90kDa urease. Three peptides unique to the JBURE-II/-IIb protein were detected by mass spectrometry in seed extracts, indicating that jbure-II/-IIb is a functional gene. Comparative modeling indicates that JBURE-IIb urease has an overall shape almost identical to C. ensiformis major urease JBURE-I with all residues critical for urease activity. The cDNA was cloned into the pET101 vector and the recombinant protein was produced in Escherichia coli. The JBURE-IIb protein, although enzymatically inactive presumably due to the absence of Ni atoms in its active site, impaired the growth of a phytopathogenic fungus and showed entomotoxic properties, inhibiting diuresis of Rhodnius prolixus isolated Malpighian tubules, in concentrations similar to those reported for JBURE-I and canatoxin. The antifungal and entomotoxic properties of the recombinant JBURE-IIb apourease are consistent with a protective role of ureases in plants.
Год издания: 2011
Авторы: Fernanda Mulinari, Arlete Beatriz Becker‐Ritt, Diogo Ribeiro Demartini, Rodrigo Ligabue‐Braun, Fernanda Stanisçuaski, Hugo Verli, Rodrigo da Rocha Fragoso, E. SCHROEDER, Célia R. Carlini, Maria Fátima Grossi‐de‐Sá
Издательство: Elsevier BV
Источник: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
Ключевые слова: Microbial Applications in Construction Materials, Enzyme-mediated dye degradation, Enzyme Production and Characterization
Другие ссылки: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (HTML)
PubMed (HTML)