Role of several key residues in the catalytic activity of sucrose isomerase from Klebsiella pneumoniae NK33-98-8

Enzyme and Microbial Technology

Volumn 40, Issue 5, 2007, Pages 1221-1227

  Aroonnual, Amornrat ^a   Nihira, Takuya ^b   Seki, Tatsuji ^b   Panbangred, Watanalai ^a  

^a Mahidol University   (Thailand)

^b OSAKA UNIVERSITY   (Japan)

Author keywords

Klebsiella pneumoniae; Palatinose; Sucrose isomerase; Trehalulose

Indexed keywords

KLEBSIELLA PNEUMONIAE; PALATINOSE; SUCROSE ISOMERASE; TREHALULOSE;

CATALYSIS; CHEMICAL MODIFICATION; ESCHERICHIA COLI; PH EFFECTS; SUGAR (SUCROSE);

ENZYME KINETICS;

ASPARAGINE; CALCIUM; GLUTAMIC ACID; GLYCINE; ISOMERASE; LITHIUM; MAGNESIUM; MERCURY; PALATINOSE; SUCROSE ISOMERASE; TREHALOSE; UNCLASSIFIED DRUG;

AMINO ACID ANALYSIS; ARTICLE; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME SPECIFICITY; ESCHERICHIA COLI; GENE OVEREXPRESSION; INHIBITION KINETICS; KLEBSIELLA PNEUMONIAE; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PH MEASUREMENT;

ESCHERICHIA COLI; KLEBSIELLA PNEUMONIAE;

EID: 33847758653     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2006.09.011     Document Type: Article

References (33)

1. Low N., and Sporns P. Analysis and quantitation of minor di- and trisaccharides in honey using capillary gas chromatography. J Food Sci 53 (1988) 558-561
2. Minami T., Fujiwara T., Ooshima T., Nakajima Y., and Hamada S. Interaction of structural isomers of sucrose in the reaction between sucrose and glucosyltransferases from mutans streptococci. Oral Microbiol Immunol 5 (1990) 189-194
3. Kawai K., Okuda Y., and Yamashita K. Changes in blood glucose and insulin after an oral palatinose administration in normal subjects. Endocrinol Jpn 32 (1985) 933-936
4. Jonker D., Lina B.A., and Kozianowski G. 13-Week oral toxicity study with isomaltulose (Palatinose) in rats. Food Chem Toxicol 40 (2002) 1383-1389
5. Asquith J., Pickering K., Trenchard-Morgan S., and Sangster S. Completion of bacterial reverse mutation test on isomaltulose (1986), Toxicol Laboratories Ltd., Ledbury, Herefordshire, UK
6. Veronese T., and Perlot P. Mechanism of sucrose conversion by the sucrose isomerase of Serratia plymuthica ATCC 15928. Enzyme Microb Technol 24 (1999) 263-269
7. Zhang D., Li X., and Zhang L.H. Isomaltulose synthase from Klebsiella sp. strain LX3: gene cloning and characterization and engineering of thermostability. Appl Environ Microbiol 68 (2002) 2676-2682
8. Cheetham P.S. The extraction and mechanism of a novel isomaltulose-synthesizing enzyme from Erwinia rhapontici. Biochem J 220 (1984) 213-220
9. Wu L., and Birch R.G. Characterization of the highly efficient sucrose isomerase from Pantoea dispersa UQ68J and cloning of the sucrose isomerase gene. Appl Environ Microbiol 71 (2005) 1581-1590
10. Miyata Y., Sugitani T., Tsuyuki K., Ebashi T., and Nakajima N. Isolation and characterization of Pseudomonas mesoacidophila producing trehalulose. Biosci Biotechnol Biochem 54 (1992) 1680-1681
11. Nagai-Miyata J., Tsuyuki K., Sugitani T., Ebashi T., and Nakajima N. Isolation and characterization of a trehalulose-producing strain of Agrobacterium. Biosci Biotechnol Biochem 57 (1993) 2049-2053
12. Zhang D., Li N., Swaminathan K., and Zhang L.H. A motif rich in charged residues determines product specificity in isomaltulose synthase. FEBS Lett 534 (2003) 151-155
13. Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 280 (1991) 309-316
14. Uitdehaag J.C., Mosi R., Kalk K.H., van der Veen B.A., Dijkhuizen L., Withers S.G., et al. X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family. Nat Struct Biol 6 (1999) 432-436
15. Janecek S. Parallel β/α-barrels of α-amylase, cyclodextrin glycosyltransferase and oligo-1,6-glucosidase versus the barrel of β-amylase: evolutionary distance is a reflection of unrelated sequences. FEBS Lett 353 (1994) 119-123
16. Nakajima R., Imanaka T., and Aiba S. Comparison of amino acid sequences of 11 different α-amylases. Appl Microbiol Biotechnol 23 (1986) 355-360
17. Jespersen H.M., MacGregor E.A., Henrissat B., Sierks M.R., and Svensson B. Starch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (β/α)8-barrel domain and evolutionary relationship to other amylolytic enzymes. J Protein Chem 12 (1993) 791-805
18. Zhang D., Li N., Lok S.M., Zhang L.H., and Swaminathan K. Isomaltulose synthase (PalI) of Klebsiella sp. LX3-crystal structure and implication of mechanism. J Biol Chem 278 (2003) 35428-35434
19. Matsuura Y., Kusunoki M., Harada W., and Kakudo M. Structure and possible catalytic residues of taka-amylase A. J Biochem 95 (1984) 697-702
20. Knegtel R.M., Strokopytov B., Penninga D., Faber O.G., Rozeboom H.J., Kalk K.H., et al. Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products. J Biol Chem 270 (1995) 29256-29264
21. Nakayama A., Yamamoto K., and Tabata S. Identification of the catalytic residues of bifunctional glycogen debranching enzyme. J Biol Chem 276 (2001) 28824-28828
22. Leemhuis H., Rozeboom H.J., Dijkstra B.W., and Dijkhuizen L. The fully conserved Asp residue in conserved sequence region I of the α-amylase family is crucial for the catalytic site architecture and activity. FEBS Lett 541 (2003) 47-51
23. Sambrook J., and Russell D. Molecular cloning: a laboratory manual. 3rd ed. (2001), Cold spring Harbor Laboratory, Cold Spring Harbor, NY
24. Tsuyuki K., Sugitani T., Miyata Y., Ebashi T., and Nakajima Y. Isolation and characterization of isomaltulose and trehalulose producing bacteria from Thailand soil. J Gen Appl Microbiol 38 (1992) 483-490
25. Sanger F., Nicklen S., and Coulson A.R. DNA sequencing with chain-termination inhibitors. Proc Natl Acad Sci USA 74 (1977) 5463-5467
26. Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., and Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77 (1989) 51-59
27. 4. Nature 227 (1970) 680-685
28. Marais J.P., De Wit J.L., and Quicke G.V. A critical examination of the Nelson-Somogyi method for the determination of reducing sugars. Anal Biochem 15 (1966) 373-381
29. Bornke F., Hajirezaei M., and Sonnewald U. Cloning and characterization of the gene cluster for palatinose metabolism from the phytopathogenic bacterium Erwinia rhapontici. J Bacteriol 183 (2001) 2425-2430
30. Blackwell J.R., and Horgan R. A novel strategy for production of a highly expressed recombinant protein in an active form. FEBS Lett 295 (1991) 10-12
31. Abad M.C., Binderup K., Rios-Steiner J., Arni R.K., Preiss J., and Geiger J.H. The X-ray crystallographic structure of Escherichia coli branching enzyme. J Biol Chem 277 (2002) 42164-42170
32. Lawson C.L., van Montfort R., Strokopytov B., Rozeboom H.J., Kalk K.H., de Vries G.E., et al. 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
33. Nakayama A., Yamamoto K., and Tabata S. The role of Asp224 in conserved sequence region I of yeast glycogen debranching enzyme. Appl Biol Sci 7 (2001) 37-47