Insights into controlling role of substitution mutation, E315G on thermostability of a lipase cloned from metagenome of hot spring soil

3 Biotech

Volumn 4, Issue 2, 2014, Pages 189-196

  Sharma, Pushpender Kumar ^a,b   Kumar, Rajender ^c   Garg, Prabha ^c   Kaur, Jagdeep ^a  

^a PANJAB UNIVERSITY   (India)

^b SRI GURU GRANTH SAHIB WORLD UNIVERSITY   (India)

^c NATIONAL INSTITUTE OF PHARMACEUTICAL EDUCATION AND RESEARCH NIPER   (India)

Author keywords

Conformation; Homology modeling; Lipase; Mutagenesis; Thermostability; hydrolase fold

Indexed keywords

GLUTAMIC ACID; POLYPEPTIDE; RECOMBINANT PROTEIN; TRIACYLGLYCEROL LIPASE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME SPECIFICITY; ESCHERICHIA COLI; GENE MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SITE DIRECTED MUTAGENESIS; STRUCTURAL HOMOLOGY; THERMOSTABILITY;

EID: 84908576451     PISSN: 2190572X     EISSN: 21905738     Source Type: Journal    
DOI: 10.1007/s13205-013-0142-4     Document Type: Article

References (36)

1. Acharya P, Rajakumara E, Sankaranarayanan R, Rao NM (2004) Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase. J Mol Bio 341: 1271-1281.
2. Ahmad S, Zahid Kamal M, Sankaranarayanan R, Rao NM (2008) Thermostable Bacillus subtilis lipases: in vitro evolution and structural insight. J Mol Bio 381: 324-340.
3. Bloom JD, Labthavikul ST, Otey CR, Arnold FH (2006) Protein stability promotes evolvability. Proc Natl Acad Sci USA 103: 5869-5874.
4. Bogin O, Peretz M, Hacham Y, Korkhin Y, Frolow F, Kalb AJ, Burstein Y (1998) Enhanced thermal stability of Clostridium beijerinckii alcohol dehydrogenase after strategic substitution of amino acid residues with prolines from the homologous thermophilic Thermoanaerobacter brockii alcohol dehydrogenase. Protein Sci 7: 1156-1163.
5. Bouzas TD, Barros-Velazquez JT, Villa G (2006) Industrial applications of hyperthermophilic enzymes: a review. Prot Pept Lett 13: 445-451.
6. Carrasco-López C, Godoy C, Rivas B, Fernández-Lorente G, Palomo JM, Guisán JM, Fernández-Lafuente R, Martínez-Ripoll M, Hermoso JA (2009) Activation of bacterial thermoalkalophilic lipases is spurred by dramatic structural rearrangements. J Biol Chem 284: 4365-4372.
7. Cherukuvada SL, Seshasayee ASN, Raghunathan K, Anishetty S, Pennathur G (2005) Evidence of a Double-Lid Movement in Pseudomonas aeruginosa lipase: insights from molecular dynamics simulations. PLoS Comput Biol 1: e28.
8. Choi WC, Kim MH, Ro HS, Sang RR, Oh TK, Lee JK (2005) Zinc in lipase L1 from Geobacillus stearothermophilus L1 and structural implications on thermal stability. FEBS Lett 579: 3461-3466.
9. Ding YF, Dokholyan NV (2007) Eris: an automated estimator of protein stability. Nat Methods 4: 466-467.
10. Fujii R, Nakagawa Y, Hiratake J, Sogabe A, Sakata K (2005) Directed evolution of Pseudomonas aeruginosa lipase for improved amide-hydrolyzing activity. Protein Eng Des Sel 18: 93-101.
11. Gromiha MM (2001) Important inter-residue contacts for enhancing the thermal stability of thermophilic proteins. Biophy Chem 91: 71-77.
12. Haney P, Konisky J, Koretke KK, Luthey-Schulten Z, Wolynes PG (1997) Structural basis for thermostability and identification of potential active site residues for adenylate kinases from the archaeal genus Methanococcus. Proteins 28: 117-130.
13. Jaeger KE, Dijkstra BW, Reetz MT (1999) Bacterial biocatalysts; molecular biology, three dimensional structures, and biotechno- biogical applications of lipases. Ann Rev Microbiol 53: 315-351.
14. Jeong ST, Kim HK, Kim JS, Chi SW, Pan JG, Oh TK, Ryu SE (2002) Novel zinc-binding center and a temperature switch in the Bacillus stearothermophilus L1 lipase. J Biol Chem 277: 17041-17047.
15. Kazlauskas RJ, Bornscheuer UT (2009) Improving enzyme properties: when are closer mutations better? Nat Chem Biol 5: 526-529.
16. Kim HK, Park SY, Oh TK, Lee JK (1998) Gene cloning and characterization of thermostable lipase from Bacillus stearothermophilus L1. Biosci Biotechnol Biochem 62: 66-71.
17. Koga Y, Kato K, Nakano H, Yamane T (2003) Inverting enantioselectivity of Burkholderia cepacia KWI-56 lipase by combinatorial mutation and high-throughput screening using single-molecule PCR and in vitro expression. J Mol Bio 331: 585-592.
18. Kumar S, Ma B, Tsai CJ, Nussinov R (2000) Electrostatic strengths of salt bridges in thermophilic and mesophilic glutamate dehydrogenase monomers. Prot Str Funct Bioinfo 38: 368-383.
19. Lindahl E, Hess B, van Der DS (2001) GROMACS: a package for molecular simulation and rajectory analysis. J Mol Model 7: 306-317.
20. Lutz S, Bornscheuer UT (2009) Protein engineering handbook, 2nd edn. Wiley VCH, Weinheim.
21. Magnusson O, Takwa M, Harnberg A, Hult K (2005) An S-selective lipase was created by rational redesign and the enantioselectivity increased with temperature. Angew Chem Int Ed 44: 4582-4585.
22. Morley KL, Kazlauskas RJ (2005) Improving enzyme properties: when are closer mutations better? Trends Biotechnol 23: 231-237.
23. Offman MN, Krol M, Patel N, Krishnan S, Liu J, Saha V, Bates PA (2011) Rational engineering of l-asparaginase reveals importance of dual activity for cancer cell toxicity. Blood 117: 1614-1621.
24. Ollis DL, Cheah E, Cygler M, Dijkstra B, Frolow F, Franken SM, Harel M, Remington SJ, Silman I, Schrag J, Sussman JL, Verschueren KHG, Goldman A (1992) The alpha/beta hydrolase fold. Protein Eng 5: 197-211.
25. Reetz MT (2000) Evolution in the test tube as a means to create enantioselective enzymes for use in organic synthesis. Sci Progr 83: 157-172.
26. Sadeghi M, Naderi-Manesh H, Zarrabi M, Ranjbar B (2006) Effective factors in thermostability of thermophilic proteins. Biophy Chem 119: 256-270.
27. Sali A, Potterton L, Feng Y, Herman V, Martin K (1995) Evaluation of comparative protein modeling by Modeller. Protein: Str Funct Genet 23: 318-326.
28. Schrag JD, Cygler M (1997) Lipases and alpha/beta hydrolase fold. Methods Enzymol 284: 85-107.
29. Sharma PK, Capalash N, Kaur J (2007) An improved method for single step purification of metagenomic DNA. Mol Biotechnol 36: 61-63.
30. Sharma PK, Singh K, Singh R, Capalash N, Ali A, Mohammad O, Kaur J (2012a) Characterization of a thermostable lipase showing loss of secondary structure at ambient temperature. Mol Biol Rep 39: 2795-2804.
31. Sharma PK, Kumar R, Kumar R, Mohammad O, Singh R, Kaur J (2012b) Engineering of a metagenome derived lipase towards thermal tolerance: effect of asparagines to lysine mutation on the protein surface. Gene 491: 264-271.
32. Shimotohno A, Oue S, Yano T, Kuramitsu S, Kagamiyama R (2001) Demonstration of the importance and usefulness of manipulating non-active-site residues in protein design. J Biochem 129: 943-948.
33. Sigurgisladottir S, Konraosdottir M, Jonsson A, Kristjansson JK, Matthiasson E (1993) Lipase activity of thermophilic bacteria from icelandic hot springs. Biotechnol Lett 15: 361-366.
34. Spiller B, Gershenson A, Arnold F, Stevens RA (1999) Structural view of evolutionary divergence. Proc Natl Acad Sci USA 96: 12305-12310.
35. Takase K (1993) Effect of mutation of an amino acid residue near the catalytic site on the activity of Bacillus stearothermophilus amylase. Eur J Biochem 211: 899-902.
36. Tokuriki N, Tawfik D (2009) Protein dynamism and evolvability. Science 324: 203-207.