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International Journal of Current Advanced Research ISSN: O: 2319-6475, ISSN: P: 2319 – 6505, Impact Factor: SJIF: 5.438 Available Online at www.journalijcar.org Volume 6; Issue 2; February 2017; Page No. 2131-2138 Research Article A COMPARATIVE ANALYSIS OF THERMOPHILIC AND PSYCHROPHILIC METALLOPEPTIDASES: INVOLVEMENT OF BIOINFORMATIC APPROACH Anuprabha1., AbhigyanNath2 and Radha Chaube3* 1,2 3Bioinformatic Division, MahilaMahavidyalya, Banaras Hindu University, Varanasi-221005, Uttar Pradesh, India ARTICLEDepartment INFO of Zoology, Institute of Science,ABSTRACT Banaras Hindu University, Varanasi-221005, Uttar Pradesh, India The thermolysin family of enzymes is classified as the M4 family of metallopeptidases. M4 Article History: family comprises numerous zinc-dependent metallopeptidases that hydrolyze peptide Received 9th November, 2016 bonds. Zinc containing peptidases are widely distributed in nature and have important roles Received in revised form 12thDecember, 2016 in many physiological processes. M4 family comprises numerous zinc-dependent Accepted 5th January, 2017 metallopeptidases that hydrolyse peptide bonds. Metallopeptidases were studied for the Published online 28th February, 2017 reason of their great relevance to biology, medicine and biotechnology. In the present study, detailed comparative analyses of both thermophilic and psychrophilic metallopeptidases were performed. The comparative analysis of both thermophilic and Key words: psychrophilic metallopeptidases was performed by taking sequence parameters such as Thermophilic, Psychrophilic, amino acid composition, amino acid property group composition, physico-chemical Metallopeptidases, amino acid residues, properties, secondary structure content. From comparison between the two groups, it was analysis found that Gln, Asn, Ser, Thr, and His are significantly lower in thermophilic metallopeptidase. Positively charged residues (Lys, Arg and Glu) are more significant in thermophilic metallopeptidases than in psychrophilic metallopeptidases.
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