Molecular cloning and biochemical characterization of the first archaeal maltogenic amylase from the hyperthermophilic archaeon Thermoplasma volcanium GSS1

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1774, Issue 5, 2007, Pages 661-669

  Kim, Jung Woo ^a,c   Kim, Yung Hee ^a   Lee, Hee Seob ^a   Yang, Sung Jae ^a   Kim, Young Wan ^a   Lee, Myoung Hee ^a   Kim, Jung Wan ^b   Seo, Nam Seok ^c   Park, Cheon Seok ^d   Park, Kwan Hwa ^a  

^a Seoul National University   (South Korea)

^b SolarLight Ltd   (South Korea)

^c Samlip General Food   (South Korea)

^d Kyung Hee University   (South Korea)

Author keywords

Maltogenic amylase; Oligomeric state; Subsite structure; Thermoplasma volcanium; Thermostability

Indexed keywords

AMYLASE; BACTERIAL ENZYME; CYCLODEXTRIN; GLYCOSIDASE; HYDROLASE; RECOMBINANT ENZYME;

ARCHAEBACTERIUM; ARTICLE; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME STRUCTURE; ESCHERICHIA COLI; GEL PERMEATION CHROMATOGRAPHY; GENE EXPRESSION; GLYCOSYLATION; MOLECULAR CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE; THERMOPLASMA; THERMOPLASMA VOLCANIUM; THERMOSTABILITY;

AMINO ACID SEQUENCE; AMYLASES; ARCHAEA; BASE SEQUENCE; CATALYSIS; CLONING, MOLECULAR; DNA PRIMERS; ENZYME STABILITY; GLYCOSYLATION; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY, AMINO ACID;

ARCHAEA; BACTERIA (MICROORGANISMS); THERMOPLASMA VOLCANIUM;

EID: 34247614099     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2007.03.010     Document Type: Article

References (36)

1. Ladenstein R., and Antranikian G. Proteins from hyperthermophiles: stability and enzymatic catalysis close to the boiling point of water. Adv. Biochem. Eng. Biotechnol. 61 (1998) 37-85
2. Bauer M.W., Driskill L.D., and Kelly R.M. Glycosyl hydrolase from hyperthermophilic microorganisms. Curr. Opin. Biotechnol. 9 (1998) 141-145
3. Vieille C., and Zeikus G.J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 65 (2001) 1-43
4. Radianingtyas H., and Wright P.C. Alcohol dehydrogenases from thermophilic and hyperthermophilic archaea and bacteria. FEMS Microbiol. Rev. 27 (2003) 593-616
5. Robinson-Rechavi M., Alibes A., and Godzik A. Contribution of electrostatic interactions, compactness and quaternary structure to protein thermostability: lessons from structural genomics of Thermotoga maritima. J. Mol. Biol. 356 (2006) 547-557
6. Park K.H., Kim T.J., Cheong T.K., Kim J.W., Oh B.H., and Svensson B. Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the α-amylase family. Biochim. Biophys. Acta 1478 (2000) 165-185
7. Hondoh H., Kuriki T., and Matsuura Y. Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase. J. Mol. Biol. 326 (2003) 177-188
8. Kamitori S., Abe A., Ohtaki A., Kaji A., Tonozuka T., and Sakano Y. Crystal structures and structural comparison of Thermoactinomyces vulgaris R-47 α-amylase I (TVAI) at 1.6 Å resolution and α-amylase II (TVAII) at 2.3 A resolution. J. Mol. Biol. 318 (2002) 443-453
9. Kim J.S., Cha S.S., Kim H.J., Kim T.J., Ha N.C., Oh S.T., Cho H.S., Cho M.J., Kim M.J., Lee H.S., Kim J.W., Choi K.Y., Park K.H., and Oh B.H. Crystal structure of a maltogenic amylase provides insights into a catalytic versatility. J. Biol. Chem. 274 (1999) 26279-26286
10. Lee H.S., Kim M.S., Cho H.S., Kim J.I., Kim T.J., Choi J.H., Park C., Oh B.H., and Park K.H. Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other. J. Biol. Chem. 277 (2002) 21891-21897
11. Kandra L., Remenyik J., Batta G., Somsak L., Gyemant G., and Park K.H. Enzymatic synthesis of a new inhibitor of α-amylases: acarviosinyl-isomaltosyl-spiro-thiohydantoin. Carbohydr. Res. 340 (2005) 1311-1317
12. Li D., Park S.H., Shim J.H., Lee H.S., Tang S.Y., Park C.S., and Park K.H. In vitro enzymatic modification of puerarin to puerarin glycosides by maltogenic amylase. Carbohydr. Res. 339 (2004) 2789-2797
13. Segerer A., Langworthy T.A., and Stetter K.O. Thermoplasma acidophilum and Thermoplasma volcanium sp. nov. from solfatara fields. Syst. Appl. Microbiol. 10 (1988) 161-171
14. Kawashima T., Yamamoto Y., Aramaki H., Nunoshiba T., Kawamoto T., Watanabe K., Yamazaki M., Kanehori K., Amano N., Ohya Y., Makino K., and Suzuki M. Determination of the complete genomic DNA sequence of Thermoplasma volcanium GSS1. Proc. Jpn. Acad. 75 (1999) 213-218
15. Sambrook J., Fritsch E.F., and Maniatis T. Molecular Cloning: A Laboratory Manual. 2nd ed. (1989), Cold Spring Harbor Laboratory Press, New York
16. Kim Y.W., Lee S.S., Warren R.A.J., and Withers S.G. Directed evolution of a glycosynthase from Agrobacterium sp. increases its catalytic activity dramatically and expands its substrate repertoire. J. Biol. Chem. 279 (2004) 42787-42793
17. Kim T.J., Kim M.J., Kim B.C., Kim J.C., Cheong T.K., Kim J.W., and Park K.H. Modes of action of acarbose hydrolysis and transglycosylation catalyzed by a thermostable maltogenic amylase, the gene for which was cloned from a Thermus strain. Appl. Environ. Microbiol. 65 (1999) 1644-1651
18. Bradford M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
19. Miller G.L. Use of dinitrosalycylic acid reagent for determination reducing sugar. Anal. Chem. 31 (1959) 426-428
20. Dayal U., and Mehta S.K. Studies on molecular weight determination using refractive index and multi-angle laser light scattering detectors in size exclusion chromatography. J. Liq. Chromatogr. 17 (1994) 303-316
21. Park S.H., Cha H., Kang H.K., Shim J.H., Woo E.J., Kim J.W., and Park K.H. Mutagenesis of Ala290, which modulates substrate subsite affinity at the catalytic interface of dimeric ThMA. Biochim. Biophys. Acta 1751 (2005) 170-177
22. Suganuma T., Matsuno R., Ohnishi M., and Hiromi K. A study of the mechanism of action of Taka-amylase A on linear oligosaccharides by product analysis and computer simulation. J. Biochem. 84 (1978) 293-316
23. Suganuma T., Ohnishi M., Hiromi K., and Nagahama T. Elucidation of the subsite structure of bacterial saccharifying (α-amylase and its mode of degradation of maltose. Carbohydr. Res. 282 (1996) 171-180
24. Kim T.J., Nguyen V.D., Lee H.S., Kim M.J., Cho H.Y., Kim Y.W., Moon T.W., Park C.S., Kim J.W., Oh B.H., Lee S.B., Svensson B., and Park K.H. Modulation of the multisubstrate specificity of Thermus maltogenic amylase by truncation of the N-terminal domain and by a salt-induced shift of the monomer/dimer equilibrium. Biochemistry 40 (2001) 14182-14190
25. Lee H.S., Kim J.S., Shim K., Kim J.W., Inouye K., Oneda H., Kim Y.W., Cheong K.A., Cha H., Woo E.J., Auh J.H., Lee S.J., Kim J.W., and Park K.H. Dissociation/association properties of a dodecameric cyclomaltodextrinase. Effects of pH and salt concentration on the oligomeric state. FEBS J. 273 (2006) 109-121
26. Tanaka Y., Tsumoto K., Yasutake Y., Umetsu M., Yao M., Fukada H., Tanaka I., and Kumagai I. How oligomerization contributes to the thermostability of an archaeon protein. Protein l-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii. J. Biol. Chem. 279 (2004) 32957-32967
27. Natalello A., Doglia S.M., Carey J., and Grandori R. Role of flavin mononucleotide in the thermostability and oligomerization of Escherichia coli stress-defense protein WrbA. Biochemistry 46 (2007) 543-553
28. Davis G.J., Wilson K.S., and Henrissat B. Nomenclature for sugar-binding subsites in glycosyl hydrolylases. Biochem. J. 321 (1997) 557-559
29. Yang S.J., Lee H.S., Park C.S., Kim Y.R., Moon T.W., and Park K.H. 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. Environ. Microbiol. 70 (2004) 5988-5995
30. Lee M.H., Kim Y.W., Kim T.J., Park C.S., Kim J.W., Moon T.W., and Park K.H. A novel amylolytic enzyme from Thermotoga maritima, resembling cyclodextrinase and α-glucosidase, that liberates glucose from the reducing end of the substrates. Biochem. Biophys. Res. Commun. 295 (2002) 818-825
31. Walden H., Taylor G., Lilie H., Knura T., and Hensel R. Triosephosphate isomerase of the hyperthermophile Thermoproteus tenax: thermostability is not everything. Biochem. Soc. Trans. 32 (2004)
32. Kim Y.W., Kim D.K., Kim M.J., Cha H., Park C.S., Moon T.W., and Park K.H. Engineering Thermus maltogenic amylase with improved thermostability: Proving the role of the conserved calcium binding site in cyclodextrin-degrading enzymes. J. Appl. Glycosci. 52 (2005) 7-13
33. Kim T.J., Park C.S., Cho H.Y., Cha S.S., Kim J.S., Lee S.B., Moon T.W., Kim J.W., Oh B.H., and Park K.H. Role of the glutamate 332 residue in the transglycosylation activity of Thermus Maltogenic amylase. Biochemistry 39 (2000) 6773-6780
34. Kandra L., Gyemant G., Remenyik J., Ragunath C., and Ramasubbu N. Subsite mapping of human salivary α-amylase and the mutant Y151M. FEBS Lett. 544 (2003) 194-198
35. Gyemant G., Hovanszki G., and Kandra L. Subsite mapping of the binding region of α-amylases with a computer program. Eur. J. Biochem. 269 (2002) 5157-5162
36. Shimura Y., Wang Q., and Sakano Y. Subsite structure of a-amylase II from Thermoactinomyces vulgaris R-47. Biosci. Biotechnol. Biochem. 63 (1999) 2199-2201