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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 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.