Comprehensive characterization and molecular insights into the salt tolerance of a Cu, Zn-superoxide dismutase from an Indian Mangrove, Avicennia marina.

ABSTRACT: Superoxide dismutases are important group of antioxidant metallozyme and play important role in ROS homeostasis in salinity stress. The present study reports the biochemical properties of a salt-tolerant Cu, Zn-superoxide from Avicennia marina (Am_SOD). Am_SOD was purified from the leaf and identified by mass-spectrometry. Recombinant Am_SOD cDNA was bacterially expressed as a homodimeric protein. Enzyme kinetics revealed a high substrate affinity and specific activity of Am_SOD as compared to many earlier reported SODs. An electronic transition in 360-400 nm spectra of Am_SOD is indicative of Cu²⁺-binding. Am_SOD activity was potentially inhibited by diethyldithiocarbamate and H₂O₂, a characteristic of Cu, Zn-SOD. Am_SOD exhibited conformational and functi

SUBMITTER: Sarkar RK 

PROVIDER: S-EPMC8810880 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature