Isolation and characterization of the gene encoding the starch debranching enzyme limit dextrinase from germinating barley

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1431, Issue 2, 1999, Pages 538-546

  Kristensen, Michael ^a   Lok, Finn ^a   Planchot, Véronique ^a   Svendsen, Ib ^a   Leah, Robert ^a   Svensson, Birte ^a  

^a CARLSBERG LABORATORY   (Denmark)

Author keywords

Genomic sequence; Glycoside hydrolase family 13; Hordeum vulgare; Limit dextrinase; Protein sequence; Pullulanase; R enzyme; Single gene

Indexed keywords

GLYCOSIDASE; OLIGO 1,6 GLUCOSIDASE; PULLULANASE; STARCH;

AMINO ACID SEQUENCE; ARTICLE; BARLEY; CATALYSIS; CONTROLLED STUDY; EXON; GENE EXPRESSION; GENE ISOLATION; GENE SEQUENCE; GERMINATION; INTRON; KLEBSIELLA; LASER; MASS SPECTROMETRY; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; RICE; SEQUENCE ANALYSIS; SOUTHERN BLOTTING; SPINACH;

AMINO ACID SEQUENCE; GENOMIC LIBRARY; GLYCOSIDE HYDROLASES; HORDEUM; MOLECULAR SEQUENCE DATA; SEQUENCE ALIGNMENT;

EID: 0032920149     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00077-1     Document Type: Article

References (33)

1. MacGregor A.W. α-Amylase, limit dextrinase, and α-glucosidase enzymes in barley and malt. CRC Crit. Rev. Biotechnol. 5:1987;117-128.
2. Hardie D.G. Control of carbohydrase formation by gibberellic acid in barley endosperms. Phytochemistry. 14:1975;1719-1722.
3. Lee W.J., Pyler R.E. Barley limit dextrinase: varietal, environmental and malting effects. J. Am. Soc. Brew. 42:1984;11-17.
4. Fincher G.B. Molecular and cellular biology associated with endosperm mobilization in germinating cereals. Annu. Rev. Plant Physiol. 40:1989;305-346.
5. M. Kristensen, B. Svensson, J. Larsen, Purification and Characterization of Barley Limit Dextrinase During Malting, Proceedings of the 24th Congress, European Brewery Convention, Oslo, Norway, IRL Press, 1993, pp. 37-43.
6. Macri L.J., MacGregor A.W., Schroeder S.W., Bazin S.L. Detection of a limit dextrinase inhibitor in barley. J. Cereal Sci. 18:1993;103-106.
7. Nakamura Y., Umemoto T., Ogata N., Kuboki Y., Yano M., Sasaki T. Starch debranching enzyme (R-enzyme or pullulanase) from developing rice endosperm: purification, cDNA and chromosomal location. Planta. 199:1996;209-218.
8. James M.G., Robertson D.S., Myers A.M. Characterization of the maize gene sugary1, a determinant of starch composition in kernels. Plant Cell. 7:1995;417-429.
9. Francisco P.B., Zhang Y., Park S., Ogata N., Yamanouchi H., Nakamura Y. Genomic DNA sequence of a rice gene coding for a pullulanase-type of starch debranching enzyme. Biochem. Biophys. Acta. 1387:1998;469-477.
10. Beatty M.K., Myers A.M., James M.G. Genomic nucleotide sequence of a full-length wild-type allele of the maize sugary1 (Su1) gene. Plant Phys. 115:1997;1731.
11. 8-barrel domain and evolutionary relationship to other amylolytic enzymes. J. Protein Chem. 12:1993;791-805.
12. Jespersen H.M., MacGregor E.A., Sierks M.R., Svensson B. Comparison of the domain level organization of starch hydrolases and related enzymes. Biochem. J. 280:1991;51-55.
13. Svensson B. Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Mol. Biol. 25:1994;141-157.
14. Davies G., Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure. 3:1995;853-859.
15. J. Sambrook, E.F. Fritsch, T. Maniatis, Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, 1989.
16. Sissons M.J., Lance R.C.M., Sparrow D.H.B. Studies on limit dextrinase in barley. 3. Limit dextrinase in developing kernels. J. Cereal Sci. 17:1993;19-24.
17. M. Kristensen, J. Abe, J. Larsen, J. Mundy, B. Svensson, Barley limit dextrinase during malting and seed development, in: F. Meuser, D.J. Manners, W. Seibel (Eds.), Progress in Plant Polymeric Carbohydrate Research, Behrs, Hamburg, 1995, pp. 19-20.
18. P. Bower, Cloned Pullulanase from Rice, Patent no. WO95/09922 (1995).
19. Kristensen M., Planchot V., Abe J., Svensson B. Large-scale purification and characterization of barley limit dextrinase, a member of the α-amylase structural family. Cereal Chem. 75:1998;473-479.
20. Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1997;1-6.
21. Henrissat B., Bairoch A. New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 316:1996;695-696.
22. Kadziola A., Abe J., Svensson B., Haser R. Crystal and molecular structure of barley α-amylase. J. Mol. Biol. 239:1994;104-121.
23. Katsuya Y., Mezaki Y., Kubota M., Matsuura Y. Three-dimensional structure of Pseudomonas isoamylase at 2.2 Å resolution. J. Mol. Biol. 281:1998;885-897.
24. Machius M., Wiegand G., Huber R. Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution. J. Mol. Biol. 246:1995;545-559.
25. Qian M., Haser R., Payan F. Structure and molecular model refinement of pig pancreatic α-amylase at 2.1 Å resolution. J. Mol. Biol. 231:1993;785-799.
26. Watanabe K., Hata Y., Kizaki H., Katsube Y., Suzuki Y. The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Å resolution: structural characterization of proline-substitution sites for protein thermostabilization. J. Mol. Biol. 269:1997;142-153.
27. Matsuura Y., Kusunoki M., Harada W., Kakudo M. Structure and possible catalytic residues of Taka-amylase A. J. Biochem. (Tokyo). 95:1984;697-702.
28. Søgaard M., Kadziola A., Haser R., Svensson B. Site-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch binding site in barley α-amylase 1. J. Biol. Chem. 268:1993;22480-22484.
29. Klein C., Schulz G.E. Structure of cyclodextrin glucosyltransferase refined at 2.0 Å resolution. J. Mol. Biol. 217:1991;737-750.
30. Kuriki T., Park J., Imanaka T. Characteristics of thermostable pullulanase from Bacillus stearothermophilus and the nucleotide sequence of the gene. J. Ferm. Bioeng. 69:1990;204-210.
31. Kuriki T., Imanaka T. Nucleotide sequence of the neopullulanase gene from Bacillus stearothermophilus. J. Gen. Microbiol. 135:1989;1521-1528.
32. Melasniemi H., Paloheimo M., Heimo L. Nucleotide sequence of the α-amylase-pullulanase gene from Clostridium thermohydrosulfuricum. J. Gen. Microbiol. 136:1990;447-454.
33. Baecker P.A., Greenberg E., Preiss J. Biosynthesis of bacterial glycogen. J. Biol. Chem. 261:1986;8738-8743.