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Braz. j. microbiol ; 45(2): 603-611, Apr.-June 2014. ilus, tab
Article in English | LILACS | ID: lil-723124

ABSTRACT

Glucose dehydrogenase (GDH; EC 1.1. 5.2) is the member of quinoproteins group that use the redox cofactor pyrroloquinoline quinoine, calcium ions and glucose as substrate for its activity. In present study, Leclercia sp. QAU-66, isolated from rhizosphere of Vigna mungo, was characterized for phosphate solubilization and the role of GDH in plant growth promotion of Phaseolus vulgaris. The strain QAU-66 had ability to solubilize phosphorus and significantly (p < 0.05) promoted the shoot and root lengths of Phaseolus vulgaris. The structural determination of GDH protein was carried out using bioinformatics tools like Pfam, InterProScan, I-TASSER and COFACTOR. These tools predicted the structural based functional homology of pyrroloquinoline quinone domains in GDH. GDH of Leclercia sp. QAU-66 is one of the main factor that involved in plant growth promotion and provides a solid background for further research in plant growth promoting activities.


Subject(s)
Enterobacteriaceae/enzymology , Enterobacteriaceae/physiology , Glucose 1-Dehydrogenase/genetics , Nerve Growth Factors , Phaseolus/growth & development , Phaseolus/microbiology , Cluster Analysis , Computational Biology , Cytosol/chemistry , DNA, Bacterial/chemistry , DNA, Bacterial/genetics , Enterobacteriaceae/genetics , Enterobacteriaceae/isolation & purification , Glucose 1-Dehydrogenase/chemistry , Models, Molecular , Molecular Sequence Data , Phylogeny , Protein Conformation , Protein Structure, Tertiary , Phosphorus/metabolism , Plant Roots/growth & development , Plant Shoots/growth & development , Quinones/analysis , Sequence Analysis, DNA , Sequence Homology
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