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Please use this identifier to cite or link to this item: http://purl.org/purl/4019

Title: Molecular cloning and homology modelling of a subtilisin-like serine protease from the marine fungus, Engyodontium album BTMFS10
Authors: Sarita,G Bhat
Jasmin, C
Sreeja, Chellappan
Rajeev, K Sukumaran
Elyas, K K
Chandrasekaran, M
Keywords: Engyodontium album
Alkaline serine protease
Homology modelling
Issue Date: 10-Jan-2010
Publisher: Springer
Abstract: An alkaline protease gene (Eap) was isolated for the first time from a marine fungus, Engyodontium album. Eap consists of an open reading frame of 1,161 bp encoding a prepropeptide consisting of 387 amino acids with a calculated molecular mass of 40.923 kDa. Homology comparison of the deduced amino acid sequence of Eap with other known proteins indicated that Eap encode an extracellular protease that belongs to the subtilase family of serine protease (Family S8). A comparative homology model of the Engyodontium album protease (EAP) was developed using the crystal structure of proteinase K. The model revealed that EAP has broad substrate specificity similar to Proteinase K with preference for bulky hydrophobic residues at P1 and P4. Also, EAP is suggested to have two disulfide bonds and more than two Ca2? binding sites in its 3D structure; both of which are assumed to contribute to the thermostable nature of the protein.
Description: World J Microbiol Biotechnol (2010) 26:1269–1279 DOI 10.1007/s11274-009-0298-6
URI: http://dyuthi.cusat.ac.in/purl/4019
Appears in Collections:Dr. Sarita G Bhat

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