Molecular cloning and homology modelling of a subtilisin-like serine protease from the marine fungus, Engyodontium album BTMFS10

Content Provider	CUSAT-Thesis
Author	Sarita, G. Bhat Jasmin, C. Sreeja, Chellappan Rajeev, K. Sukumaran Elyas, K. K. Chandrasekaran, M.
Abstract	An alkaline protease gene (Eap) was isolatedfor the first time from a marine fungus, Engyodontiumalbum. Eap consists of an open reading frame of 1,161 bpencoding a prepropeptide consisting of 387 amino acidswith a calculated molecular mass of 40.923 kDa. Homologycomparison of the deduced amino acid sequence ofEap with other known proteins indicated that Eap encodean extracellular protease that belongs to the subtilasefamily of serine protease (Family S8). A comparativehomology model of the Engyodontium album protease(EAP) was developed using the crystal structure of proteinaseK. The model revealed that EAP has broad substratespecificity similar to Proteinase K with preference forbulky hydrophobic residues at P1 and P4. Also, EAP issuggested to have two disulfide bonds and more than twoCa2? binding sites in its 3D structure; both of which areassumed to contribute to the thermostable nature of theprotein.
File Format	PDF
Language	English
Publisher	Springer
Access Restriction	Open
Subject Keyword	Engyodontium album Alkaline serine protease Subtilases Homology modelling
Content Type	Text
Resource Type	Article