Abstract

MOLECULAR STRUCTURAL AND DOCKING ANALYSIS OF ENOLASE PROTEIN IN AUSTRUCA ANNULIPES

S. Haritha and Dr. K. Shoba*

ABSTRACT

Fiddler crabs have a variety of adaptations for life on land, and they also exhibit remarkably complex behaviour and adaptability for an invertebrate. Fiddler crabs, which are widespread throughout the world's tropics and subtropics, are members of the Ocypodidae family and subfamily Ucinae. Common intertidal habitats for fiddler crabs include muddy or sandy open flats of protected beaches, river banks, salt marshes, and mangrove muck. The enlarged pincer of Austruca annulipes is often pink, but occasionally virtually white. The longer pincer of the male fiddler crab is almost twice as wide as its body. The male fiddler crab's enlarged pincer almost twice as long as the body width. Enolase, a crucial glycolytic enzyme, is a member of a novel class of surface proteins that lack traditional surface transport machinery but are carried on the cell surface via an unidentified method. Enolase enzymes are abundantly expressed, cytosolic carbon-oxygen lyases known for their role in glucose metabolism. Recently, enolase has been shown to possess a variety of different regulatory functions, beyond glycolysis and gluconeogenesis, associated with hypoxia, ischemia, and Alzheimer’s diseases (AD). From NCBI database sequence of enolase protein in Austruca annulipes retrieved. The gene expression analysis were done using ACUA tool for enolase protein. Gene profilling followed by motif analysis were done using SMART, FGENESH, DiS EMBL and Genescan. Structural and docking analyses were done through I-TASSER and CB DOCK. This study looks at enolase (Austruca annulipes) possible applications, and the findings indicate that enolase is a prospective therapeutic target for a number of disease like hypoxia, ischemia, and Alzheimer’s (AD).

Keywords: Austruca annulipes; Atenolol; Antimicrobial proteins; Enolase; Molecular structural analysis; Docking analysis.