Dimerization Mediates Thermo-Adaptation, Substrate Affinity and Transglycosylation in a Highly Thermostable Maltogenic Amylase of Geobacillus thermoleovorans

PLoS ONE

Volumn 8, Issue 9, 2013, Pages

  Mehta, Deepika ^a   Satyanarayana, Tulasi ^a  

^a UNIVERSITY OF DELHI   (India)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMYLASE; CYCLODEXTRIN; DIMER; HOMODIMER; MONOMER; RECOMBINANT ENZYME; STARCH;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; CATALYSIS; DIMERIZATION; ENTHALPY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME REGULATION; ENZYME STABILITY; ENZYME SUBSTRATE; GEOBACILLUS THERMOLEOVORANS; GLYCOSYLATION; MOLECULAR DOCKING; MOLECULAR WEIGHT; NUCLEOTIDE SEQUENCE; PROTEIN CARBOHYDRATE INTERACTION; PROTEIN HYDROLYSIS; SITE DIRECTED MUTAGENESIS; TEMPERATURE ACCLIMATIZATION; THERMOPHILIC BACTERIUM;

DIMERIZATION; ENZYME STABILITY; GEOBACILLUS; GLYCOSIDE HYDROLASES; SUBSTRATE SPECIFICITY;

EID: 84884373635     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0073612     Document Type: Article

References (33)

1. Li F, Zhu X, Li Y, Cao H, Zhang Y, (2011) Functional characterization of a special thermophilic multifunctional amylase OPMA-N and its N-terminal domain. Acta Biochim Biophys Sin 43: 324-334.
2. Cha H-J, Yoon H-G, Kim Y-W, Lee H-S, Kim J-W, et al. (1998) Molecular and enzymatic characterization of a maltogenic amylase that hydrolyzes and transglycosylates acarbose. Eur J Biochem 253: 251-262.
3. Oh K-W, Kim M-J, Kim H-Y, Kim B-Y, Baik M-Y, et al. (2005) Enzymatic characterization of a maltogenic amylase from Lactobacillus gasseri ATCC 33323 expressed in Escherichia coli. FEMS Microbiol Lett 252: 175-181.
4. Liu B, Wang Y, Zhang X, (2006) Characterization of a recombinant maltogenic amylase from deep sea thermophilic Bacillus sp WPD616. Enz Microb Technol 39: 805-810.
5. Kolcuoǧlu Y, Colak A, Faiz O, Belduz AO, (2010) Cloning, expression and characterization of highly thermo- and pH-stable maltogenic amylase from a thermophilic bacterium Geobacillus caldoxylosilyticus TK4. Proc Biochem 45: 821-828.
6. Derde LJ, Gomand SV, Courtin CM, Delcour JA, (2012) Characterisation of three starch degrading enzymes: Thermostable β-amylase, maltotetraogenic and maltogenic α-amylases. Food Chem 135: 713-721.
7. Yang S-J, Lee H-S, Park C-S, Kim Y-R, Moon T-W, et al. (2000) Enzymatic analysis of an amylolytic enzyme from the hyperthermophilic archaeon Pyrococcus furiosus reveals its novel catalytic properties as both an α-amylase and a cyclodextrin-hydrolyzing enzyme. Appl Env Microbiol 70: 5988-5995.
8. Kim J-W, Kim Y-H, Lee H-S, Yang S-J, Kim Y-W, et al. (2007) Molecular cloning and biochemical characterization of the first archaeal maltogenic amylase from the hyperthermophilic archaeon Thermoplasma volcanium GSS1. Biochim Biophys Acta 1774: 661-669.
9. Li D, Park J-T, Li X, Kim S, Lee S, et al. (2010) Overexpression and characterization of an extremely thermostable maltogenic amylase, with an optimal temperature of 100°C, from the hyperthermophilic archaeon Staphylothermus marinus. New Biotechnol 27: 300-307.
10. Li X, Li D, Yin Y, Park K-H, (2010) Characterization of a recombinant amylolytic enzyme of hyperthermophilic archaeon Thermofilum pendens with extremely thermostable maltogenic amylase activity. Appl Microbiol Biotechnol 85: 1821-1830.
11. MacGregor EA, Janećek Š, Svensson B, (2001) Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. Biochim Biophys Acta 1546: 1-20.
12. Mehta D, Satyanarayana T, (2013) Biochemical and molecular characterization of recombinant acidic and thermostable raw-starch hydrolysing α-amylase from an extreme thermophile Geobacillus thermoleovorans. J Mol Catal B: Enzym 85-86: 229-238.
13. Li X, Yu H-Y, (2012) Purification and characterization of novel organic-solvent tolerant β-amylase and serine protease from a newly isolated Salimicrobium halophilum strain LY20. FEMS Microbiol Lett 329: 204-211.
14. Vangrysperre W, Kersters-Hilderson H, Callens M, Bruyne CKD, (1989) Reaction of Woodward's reagent K with D-xylose isomerases, Modification of an active site carboxylate residue. Biochem J 260: 163-169.
15. Bruins ME, Janssen AE, Boom RM, (2001) Thermozymes and their applications: a review of recent literature and patents. Appl Biochem Biotechnol 90: 155-186.
16. Rao JLUM, Satyanarayana T, (2007) Purification and characterization of a hyperthermostable and high maltogenic α-amylase of an extreme thermophile Geobacillus thermoleovorans. Appl Biochem Biotechnol 142: 179-193.
17. Kim T-J, Nguyen VD, Lee H-S, Kim M-J, Cho H-Y, et al. (2001) Modulation of multisubstrate specificity of Thermus maltogenic amylase by truncation of the N-terminal domain and by a salt-induced shift of the monomer/dimer equilibrium. Biochem 40: 14182-14190.
18. Park S-H, Kang H-K, Shim J-H, Woo E-J, Hong J-S, et al. (2007) Modulation of the substrate preference of Thermus maltogenic amylase by mutation of the residues at the interface of a dimer. Biosci Biotechnol Biochem 71: 1564-1567.
19. Park KH, Lee HS, Kim TJ, Cheong KA, Nguyen VD, et al. (2002) N- and C- terminal region mediated oligomerization of the cyclodextrin-/pullulan degrading enzymes. Biologia, Bratislava 57: 87-92.
20. Kim JS, Cha SS, Kim HJ, Kim TJ, Ha NC, et al. (1999) Crystal structure of a maltogenic amylase provide insights into a catalytic versatility. J Biol Chem 274: 26279-26286.
21. Kamitori S, Kondo S, Okuyama K, Yokota T, Shimura Y, et al. (1999) Crystal structure of Thermoactinomyces vulgaris R-47 α-amylase II (TVAII) hydrolyzing cyclodextrin and pullulan at 26 A° resolution. J Mol Biol 287: 907-921.
22. Del Valle EMM, (2004) Cyclodextrins and their uses: a review. Proc Biochem 39: 1033-1046.
23. Bazzicalupo M, Fani R (1995) The use of RAPD for generating specific DNA probes for microorganism. In: Clapp JP (Ed.), Methods in molecular biology, Species diagnostic protocols: PCR and other nucleic acids methods. Humana Press Inc., Totowa, NJ, 155-177.
24. GenomeNet website. Available http://www.genome.jp/tools/clustalw/ (Accessed 2013 July 10).
25. Arnold K, Bordoli L, Kopp J, Schwede T, (2006) The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling. Bioinformatics 22: 195-201.
26. Guex N, Peitsch MC, (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling. Electrophoresis 18: 2714-2723.
27. Bikadi Z, Hazai E, (2006) Application of the PM6 semi-empirical method to modeling proteins enhances docking accuracy of AutoDock. J Cheminf 1: 15.
28. Morris GM, Goodsell DS, Halliday RS, Huey R, Hart WE, et al. (1998) Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J Comput Chem 19: 1639-1662.
29. Solis FJ, Wets RJB, (1981) Minimization by random search techniques. Math Opr Res 6: 19-30.
30. Qing G, Ma L-C, Khorchid A, Swapna GVT, Mal TK, et al. (2004) Cold-shock induced high-yield protein production in Ecoli. Nature Biotechnol 22: 877-882.
31. Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
32. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ, (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193: 265-275.
33. Miller GL, (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 3: 426-428.