International Journal of Fisheries and Aquatic Studies
2020, Vol. 8, Issue 4, Part B
Cloning and sequence analysis of Astacin like metalloproteinase gene from Indian oyster, Magallana bilineata (Röding, 1798)
Author(s): Esha Arshad, MA Pradeep, EA Nisha, TS Azhar Shahansha and KK Vijayan
Abstract: Astacins are a group of zinc-dependent metalloproteases with diverse roles in biological systems such as embryonic development, connective tissue remodelling, digestion, and processing of biologically active peptides. This paper describes the cloning of an Astacin like metalloproteinase (
Mbi-ALMP) from the digestive tissues of
Magallana bilineata. The
Mbi-ALMP encodes a deduced 440 amino acid protein which includes an N-terminal signal peptide. The
Mbi-ALMP possesses several of the characteristic features of the Astacin family like the pro-peptide domain, Astacin catalytic domain with Zinc binding motif, and met-turn, followed by a MAM (meprin, A5 protein, receptor protein-tyrosine phosphatase µ) carboxy-terminal domain. Amino acid sequence alignment and phylogenetic analysis of the protease domain indicate
Mbi-ALMP to have a high degree of sequence homology to other Astacin like metalloproteases from different species.
Pages: 124-129 | 612 Views 86 DownloadsDownload Full Article: Click Here
How to cite this article:
Esha Arshad, MA Pradeep, EA Nisha, TS Azhar Shahansha, KK Vijayan. Cloning and sequence analysis of Astacin like metalloproteinase gene from Indian oyster, Magallana bilineata (Röding, 1798). Int J Fish Aquat Stud 2020;8(4):124-129.
