Functional analysis and structure determination of alkaline protease from Aspergillus flavus

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Title	Functional analysis and structure determination of alkaline protease from Aspergillus flavus
Authors	Rabbani Syed¹*, Roja Rani², Sabeena⁴, Tariq Ahmad Masoodi¹, Gowher Shafi³, Khalid Alharbi¹
Affiliation	¹College of Applied Medical Sciences, King Saud University, Riyadh, Saudi Arabia; ²Biotechnology Department,Acharya Nagarjuna University,Guntur,AP, India; ³Institute of Genetics and Hospital for Genetic Diseases, Hyderabad, India; ⁴Jawaharlal Nehru Institute of Advanced Studies, Hyderabad, India
Email	rabbanisyd@gmail.com ; *Corresponding author
Article Type	Hypothesis
Date	Received February 06, 2012; Accepted February 7, 2012; Published February 28, 2012
Abstract	Proteases are one of the highest value commercial enzymes as they have broad applications in food, pharmaceutical, detergent, and dairy industries and serve as vital tools in determination of structure of proteins and polypeptides. Multiple application of these enzymes stimulated interest to discover them with novel properties and considerable advancement of basic research into these enzymes. A broad understanding of the active site of the enzyme and of the mechanism of its inactivation is essential for delineating its structure-function relationship. Primary structure analysis of alkaline protease showed 42% of its content to be alpha helix making it stable for three dimensional structure modeling. Homology model of alkaline protease has been constructed using the X-ray structure (3F7O) as a template and swiss model as the workspace. The model was validated by ProSA, SAVES, PROCHECK, PROSAII and RMSD. The results showed the final refined model is reliable. It has 53% amino acid sequence identity with the template, 0.24 Å as RMSD and has -7.53 as Z-score, the Ramachandran plot analysis showed that conformations for 83.4 % of amino acid residues are within the most favored regions and only 0.4% in the disallowed regions.
Keywords	Alkaline Proteases, Homology Model, Ramachandran plot
Citation	*Syed et al.* Bioinformation 8(4): 175-180 (2012)
Edited by	P Kangueane
ISSN	0973-2063
Publisher	Biomedical Informatics
License	This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.