| Literature DB >> 27778111 |
Prashant Kumar Singh1, Alok Kumar Shrivastava2, Shilpi Singh1, Ruchi Rai1, Antra Chatterjee1, L C Rai3.
Abstract
In silico derived properties on experimental validation revealed that hypothetical protein Alr2954 of Anabaena sp. PCC7120 is ADP-ribose pyrophosphatase, which belongs to nudix hydrolase superfamily. Presence of ADP-ribose binding site was attested by ADP-ribose pyrophosphatase activity (K m 44.71 ± 8.043 mM, V max 7.128 ± 0.417 μmol min-1 mg protein-1, and K cat/K m 9.438 × 104 μM-1 min-1). Besides ADP-ribose, the enzyme efficiently hydrolyzed various nucleoside phosphatases such as 8-oxo-dGDP, 8-oxo-dADP, 8-oxo-dGTP, 8-oxo-dATP, GDP-mannose, ADP-glucose, and NADH. qRT-PCR analysis of alr2954 showed significant expression under different abiotic stresses reconfirming its role in stress tolerance. Thus, Alr2954 qualifies to be a member of nudix hydrolase superfamily, which serves as ADP-ribose pyrophosphatase and assists in multiple abiotic stress tolerance.Entities:
Keywords: ADP-ribose pyrophosphatase; Anabaena sp. PCC 7120; Cloning and expression; Escherichia coli; Homology modeling; Hypothetical protein; Molecular docking
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Year: 2016 PMID： 27778111 DOI： 10.1007/s10142-016-0531-y
Source DB: PubMed Journal: Funct Integr Genomics ISSN： 1438-793X Impact factor: 3.410