caa a22 4500 445818301 CHVBK 20180317145235.0 cr unu---uuuuu 170323e20110101xx s 000 0 eng 10.1007/s00792-010-0337-0 doi (NATIONALLICENCE)springer-10.1007/s00792-010-0337-0 In silico characterization of thermostable lipases [Elektronische Daten] [Debamitra Chakravorty, Saravanan Parameswaran, Vikash Dubey, Sanjukta Patra] Thermostable lipases are of high priority for industrial applications as they are endowed with the capability of carrying out diversified reactions at elevated temperatures. Extremophiles are their potential source. Sequence and structure annotation of thermostable lipases can elucidate evolution of lipases from their mesophilic counterparts with enhanced thermostability hence better industrial potential. Sequence analysis highlighted the conserved residues in bacterial and fungal thermostable lipases. Higher frequency of AXXXA motif and poly Ala residues in lid domain of thermostable Bacillus lipases were distinguishing characteristics. Comparison of amino acid composition among thermostable and mesostable lipases brought into light the role of neutral, charged and aromatic amino acid residues in enhancement of thermostability. Structural annotation of thermostable lipases with that of mesostable lipases revealed some striking features which are increment of gamma turns in thermostable lipases; being first time reported in our paper, longer beta strands, lesser beta-branched residues in helices, increase in charged-neutral hydrogen bonding pair, hydrophobic-hydrophobic contact and differences in the N-cap and C-cap residues of the α helices. Conclusively, it can be stated that subtle changes in the arrangement of amino acid residues in the tertiary structure of lipases contributes to enhanced thermostability. Springer, 2010 Thermostable lipases nationallicence Mesostable lipases nationallicence Motif nationallicence Conserved domains nationallicence Sub family nationallicence Tertiary structure nationallicence MSA : Multiple sequence alignment nationallicence TBFL : Thermostable bacterial and fungal lipases nationallicence ML : Mesostable lipases nationallicence TBL : Thermostable bacterial lipases nationallicence TFL : Thermostable fungal lipases nationallicence Chakravorty Debamitra Department of Biotechnology, Indian Institute of Technology, 781039, Guwahati, Assam, India aut Parameswaran Saravanan Department of Biotechnology, Indian Institute of Technology, 781039, Guwahati, Assam, India aut Dubey Vikash Department of Biotechnology, Indian Institute of Technology, 781039, Guwahati, Assam, India aut Patra Sanjukta Department of Biotechnology, Indian Institute of Technology, 781039, Guwahati, Assam, India aut Extremophiles Springer Japan 15/1(2011-01-01), 89-103 1431-0651 15:1<89 2011 15 792 https://doi.org/10.1007/s00792-010-0337-0 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00792-010-0337-0 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Chakravorty Debamitra Department of Biotechnology, Indian Institute of Technology, 781039, Guwahati, Assam, India aut NATIONALLICENCE 700 1- Parameswaran Saravanan Department of Biotechnology, Indian Institute of Technology, 781039, Guwahati, Assam, India aut NATIONALLICENCE 700 1- Dubey Vikash Department of Biotechnology, Indian Institute of Technology, 781039, Guwahati, Assam, India aut NATIONALLICENCE 700 1- Patra Sanjukta Department of Biotechnology, Indian Institute of Technology, 781039, Guwahati, Assam, India aut NATIONALLICENCE 773 0- Extremophiles Springer Japan 15/1(2011-01-01), 89-103 1431-0651 15:1<89 2011 15 792 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer