Engineering cyclodextrin glycosyltransferase into a starch hydrolase with a high exo-specificity

Journal of Biotechnology

Volumn 103, Issue 3, 2003, Pages 203-212

  Leemhuis, Hans ^a   Kragh, Karsten M ^b   Dijkstra, Bauke W ^a   Dijkhuizen, Lubbert ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

^b DANISCO A S   (Denmark)

Author keywords

CGTase; Endo activity; Exo activity; Maltogenic amylase; amylase

Indexed keywords

CATALYSIS; HYDROLYSIS; SUBSTRATES;

STARCH HYDROLASE;

ENZYMES;

AMYLASE; BACTERIAL ENZYME; CYCLOMALTODEXTRIN GLUCANOTRANSFERASE; HYDROLASE; STARCH;

ARTICLE; BACTERIUM; BINDING SITE; CONTROLLED STUDY; CYCLIZATION; ENZYME ACTIVITY; ENZYME SPECIFICITY; ENZYME STRUCTURE; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL;

BACILLUS STEAROTHERMOPHILUS; GEOBACILLUS STEAROTHERMOPHILUS; INSERTION SEQUENCES;

EID: 0142122892     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1656(03)00126-3     Document Type: Article

References (37)

1. Beier L., Svendsen A., Andersen C., Frandsen T.P., Borchert T.V., Cherry J.R. Conversion of the maltogenic alpha-amylase Novamyl into a CGTase. Protein Eng. 13:2000;509-513.
2. ®, a thermostable α-amylase. Starch/Stärke. 50:1998;39-45.
3. Crabb W.D., Mitchinson C. Enzymes involved in the processing of starch to sugars. Tibtech. 15:1997;349-352.
4. Dauter Z., Dauter M., Brzozowski A.M., Christensen S., Borchert T.V., Beier L., Wilson K.S., Davies G.J. X-ray structure of Novamyl, the five-domain 'maltogenic' α-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7 Å resolution. Biochemistry. 38:1999;8385-8392.
5. Diderichsen B., Christiansen L. Cloning of a maltogenic alpha-amylase from Bacillus stearothermophilus. FEMS Microbiol. Lett. 56:1988;53-60.
6. Guex N., Peitsch M.C. SWISS-MODEL and the Swiss-Pdb viewer: an environment for comparative protein modeling. Electrophoresis. 18:1997;2714-2723.
7. Haeckel K., Bahl H. Cloning and expression of the thermostable α-amylase gene from Clostridium thermosulfurigenes (DSM 3896) in Escherichia coli. FEMS Microbiol. Lett. 60:1989;333-338.
8. Hanahan D. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:1983;557-580.
9. Henrissat B., Davies G.J. Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol. 7:1997;637-644.
10. Janeeek S. α-Amylase family: molecular biology and evolution. Prog. Biophys. Mol. Biol. 25:1997;67-97.
11. Kim Y.H., Bae K.H., Kim T.J., Park K.H., Lee H.S., Byun S.M. Effect on product specificity of cyclodextrin glycosyltransferase by site-directed mutagenesis. Biochem. Mol. Biol. Int. 41:1997;227-234.
12. Klein C., Schulz G.E. Structure of cyclodextrin glycosyltransferase refined to 2.0 Å resolution. J. Mol. Biol. 217:1991;737-750.
13. Lawson C.L., van Montfort R., Strokopytov B., Rozeboom H.J., Kalk K.H., de Vries G.E., Penninga D., Dijkhuizen L., Dijkstra B.W. Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form. J. Mol. Biol. 236:1994;590-600.
14. Lazzaroni J.C., Portalier R. Isolation and preliminary characterization of periplasmic leaky mutants of Escherichia coli K-12. FEMS Microbiol. Lett. 5:1979;411-416.
15. Leemhuis H., Dijkstra B.W., Dijkhuizen L. Mechanism of Thermoanaerobacterium thermosulfurigenes CGTase: mechanism and kinetics of inhibition by acarbose and cyclodextrins. Eur. J. Biochem. 270:2002;155-162.
16. Leemhuis H., Dijkstra B.W., Dijkhuizen L. Mutations converting cyclodextrin glycosyltransferase from a transglycosylase into a starch hydrolase. FEBS Lett. 514:2002;189-192.
17. Leemhuis H., Uitdehaag J.C.M., Rozeboom H.J., Dijkstra B.W., Dijkhuizen L. The remote substrate binding subsite-6 in cyclodextrin glycosyltransferase controls the transferase activity of the enzyme via an induced-fit mechanism. J. Biol. Chem. 277:2002;1113-1119.
18. McCarter J.D., Withers S.G. Mechanisms of enzymatic glycoside hydrolysis. Curr. Opin. Struct. Biol. 4:1994;885-892.
19. Nakamura A., Haga K., Yamane K. Three histidine residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: effects of the replacement on pH dependence and transition-state stabilization. Biochemistry. 32:1993;6624-6631.
20. Nakamura A., Haga K., Yamane K. Four aromatic residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: effects of replacements on substrate binding and cyclization characteristics. Biochemistry. 33:1994;9929-9936.
21. Nakamura A., Haga K., Yamane K. The transglycosylation reaction of cyclodextrin glucanotransferase is operated by a Ping-Pong mechanism. FEBS Lett. 337:1994;66-70.
22. Olesen, T., 1991. Antistalling process and agent. Patent application WO9104669.
23. Parsiegla G., Schmidt A.K., Schulz G.E. Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the gamma-cyclodextrin production. Eur. J. Biochem. 255:1998;710-717.
24. Pedersen S., Dijkhuizen L., Dijkstra B.W., Jensen B.F., Jørgensen S.T. A better enzyme for cyclodextrins. Chemtech. 12:1995;19-25.
25. Penninga D., Strokopytov B., Rozeboom H.J., Lawson C.L., Dijkstra B.W., Bergsma J., Dijkhuizen L. Site-directed mutations in tyrosine 195 of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 affect activity and product specificity. Biochemistry. 34:1995;3368-3376.
26. Penninga D., van der Veen B.A., Knegtel R.M., van Hijum S.A.F.T., Rozeboom H.J., Kalk K.H., Dijkstra B.W., Dijkhuizen L. The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251. J. Biol. Chem. 271:1996;32777-32784.
27. Sambrook J., Frisch E.J., Maniatis T. Molecular Cloning: A Laboratory Manual. Second ed:1989;Cold Spring Harbor Laboratory Press, New York.
28. Strokopytov B., Knegtel R.M., Penninga D., Rozeboom H.J., Kalk K.H., Dijkhuizen L., Dijkstra B.W. Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 angstrom resolution. Implications for product specificity. Biochemistry. 35:1996;4241-4249.
29. Svensson B. Protein engineering in the alpha-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Mol. Biol. 25:1994;141-157.
30. Uitdehaag J.C.M., Mosi R., Kalk K.H., van der Veen B.A., Dijkhuizen L., Withers S.G., Dijkstra B.W. X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family. Nature Struct. Biol. 6:1999;432-436.
31. Uitdehaag J.C.M., van der Veen B.A., Dijkhuizen L., Elber R., Dijkstra B.W. Enzymatic circularization of a malto-octaose linear chain studied by stochastic reaction path calculations on cyclodextrin glycosyltransferase. Proteins: Struct. Funct. Genet. 43:2001;327-335.
32. van der Maarel M.J.E.C., van der Veen B.A., Uitdehaag J.C.M., Leemhuis H., Dijkhuizen L. Properties and applications of starch-converting enzymes of the α-amylase family. J. Biotechnol. 94:2002;137-155.
33. van der Veen B.A., Uitdehaag J.C.M., Dijkstra B.W., Dijkhuizen L. Engineering of cyclodextrin glycosyltransferase reaction and product specificity. Biochim. Biophys. Acta. 1543:2000;336-360.
34. van der Veen B.A., et al. Rational design of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 to increase alpha-cyclodextrin production. J. Mol. Biol. 296:2000;1027-1038.
35. van der Veen B.A., Leemhuis H., Kralj S., Uitdehaag J.C.M., Dijkstra B.W., Dijkhuizen L. Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextrin glycosyltransferase. J. Biol. Chem. 276:2001;44557-44562.
36. Vikmon, M., 1982. Rapid and simple spectrophotometric method for determination of microamounts of cyclodextrins. In: Szejlti, J. (Eds.), Proceedings of the First International Symposium on Cyclodextrins, Reidel Publishing Co., Dordrecht, The Netherlands, pp. 64-74.
37. Wind R.D., Uitdehaag J.C.M., Buitelaar R.M., Dijkstra B.W., Dijkhuizen L. Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1. J. Biol. Chem. 273:1998;5771-5779.