Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1989 Nov 15;264(1):309–311. doi: 10.1042/bj2640309

Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes.

B Svensson 1, H Jespersen 1, M R Sierks 1, E A MacGregor 1
PMCID: PMC1133580  PMID: 2481445

Full text

PDF
309

Images in this article

309Fig. 1.
on p.309

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Amemura A., Chakraborty R., Fujita M., Noumi T., Futai M. Cloning and nucleotide sequence of the isoamylase gene from Pseudomonas amyloderamosa SB-15. J Biol Chem. 1988 Jul 5;263(19):9271–9275. [PubMed] [Google Scholar]
  2. Binder F., Huber O., Böck A. Cyclodextrin-glycosyltransferase from Klebsiella pneumoniae M5a1: cloning, nucleotide sequence and expression. Gene. 1986;47(2-3):269–277. doi: 10.1016/0378-1119(86)90070-3. [DOI] [PubMed] [Google Scholar]
  3. Buisson G., Duée E., Haser R., Payan F. Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 A resolution. Role of calcium in structure and activity. EMBO J. 1987 Dec 20;6(13):3909–3916. doi: 10.1002/j.1460-2075.1987.tb02731.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Dayhoff M. O., Barker W. C., Hunt L. T. Establishing homologies in protein sequences. Methods Enzymol. 1983;91:524–545. doi: 10.1016/s0076-6879(83)91049-2. [DOI] [PubMed] [Google Scholar]
  5. Friedberg F., Rhodes C. Segments of amino acid sequence similarity in beta-amylases. Protein Seq Data Anal. 1988;1(6):499–501. [PubMed] [Google Scholar]
  6. Fujita M., Torigoe K., Nakada T., Tsusaki K., Kubota M., Sakai S., Tsujisaka Y. Cloning and nucleotide sequence of the gene (amyP) for maltotetraose-forming amylase from Pseudomonas stutzeri MO-19. J Bacteriol. 1989 Mar;171(3):1333–1339. doi: 10.1128/jb.171.3.1333-1339.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Garnier J., Osguthorpe D. J., Robson B. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. J Mol Biol. 1978 Mar 25;120(1):97–120. doi: 10.1016/0022-2836(78)90297-8. [DOI] [PubMed] [Google Scholar]
  8. Johnson L. N., Cheetham J., McLaughlin P. J., Acharya K. R., Barford D., Phillips D. C. Protein-oligosaccharide interactions: lysozyme, phosphorylase, amylases. Curr Top Microbiol Immunol. 1988;139:81–134. doi: 10.1007/978-3-642-46641-0_4. [DOI] [PubMed] [Google Scholar]
  9. Katsuragi N., Takizawa N., Murooka Y. Entire nucleotide sequence of the pullulanase gene of Klebsiella aerogenes W70. J Bacteriol. 1987 May;169(5):2301–2306. doi: 10.1128/jb.169.5.2301-2306.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kimura K., Kataoka S., Ishii Y., Takano T., Yamane K. Nucleotide sequence of the beta-cyclodextrin glucanotransferase gene of alkalophilic Bacillus sp. strain 1011 and similarity of its amino acid sequence to those of alpha-amylases. J Bacteriol. 1987 Sep;169(9):4399–4402. doi: 10.1128/jb.169.9.4399-4402.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kitamoto N., Yamagata H., Kato T., Tsukagoshi N., Udaka S. Cloning and sequencing of the gene encoding thermophilic beta-amylase of Clostridium thermosulfurogenes. J Bacteriol. 1988 Dec;170(12):5848–5854. doi: 10.1128/jb.170.12.5848-5854.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kubota M., Mikami B., Tsujisaka Y., Morita Y. Crystallization of and preliminary crystallographic data for Bacillus stearothermophilus cyclodextrin glucanotransferase. J Biochem. 1988 Jul;104(1):12–13. doi: 10.1093/oxfordjournals.jbchem.a122406. [DOI] [PubMed] [Google Scholar]
  13. Long C. M., Virolle M. J., Chang S. Y., Chang S., Bibb M. J. alpha-Amylase gene of Streptomyces limosus: nucleotide sequence, expression motifs, and amino acid sequence homology to mammalian and invertebrate alpha-amylases. J Bacteriol. 1987 Dec;169(12):5745–5754. doi: 10.1128/jb.169.12.5745-5754.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. MacGregor E. A. Alpha-amylase structure and activity. J Protein Chem. 1988 Aug;7(4):399–415. doi: 10.1007/BF01024888. [DOI] [PubMed] [Google Scholar]
  15. MacGregor E. A., Svensson B. A super-secondary structure predicted to be common to several alpha-1,4-D-glucan-cleaving enzymes. Biochem J. 1989 Apr 1;259(1):145–152. doi: 10.1042/bj2590145. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Matsuura Y., Kusunoki M., Harada W., Kakudo M. Structure and possible catalytic residues of Taka-amylase A. J Biochem. 1984 Mar;95(3):697–702. doi: 10.1093/oxfordjournals.jbchem.a134659. [DOI] [PubMed] [Google Scholar]
  17. Quiocho F. A. Carbohydrate-binding proteins: tertiary structures and protein-sugar interactions. Annu Rev Biochem. 1986;55:287–315. doi: 10.1146/annurev.bi.55.070186.001443. [DOI] [PubMed] [Google Scholar]
  18. Rogers J. C., Milliman C. Isolation and sequence analysis of a barley alpha-amylase cDNA clone. J Biol Chem. 1983 Jul 10;258(13):8169–8174. [PubMed] [Google Scholar]
  19. Stavn A., Granum P. E. Purification and physiocochemical properties of an extra-cellular cycloamylose (cyclodextrin) glucanotransferase from Bacillus macerans. Carbohydr Res. 1979 Oct;75:243–250. doi: 10.1016/s0008-6215(00)84643-1. [DOI] [PubMed] [Google Scholar]
  20. Svensson B., Larsen K., Gunnarsson A. Characterization of a glucoamylase G2 from Aspergillus niger. Eur J Biochem. 1986 Feb 3;154(3):497–502. doi: 10.1111/j.1432-1033.1986.tb09425.x. [DOI] [PubMed] [Google Scholar]
  21. Svensson B. Regional distant sequence homology between amylases, alpha-glucosidases and transglucanosylases. FEBS Lett. 1988 Mar 28;230(1-2):72–76. doi: 10.1016/0014-5793(88)80644-6. [DOI] [PubMed] [Google Scholar]
  22. Takahashi T., Kato K., Ikegami Y., Irie M. Different behavior towards raw starch of three forms of glucoamylase from a Rhizopus sp. J Biochem. 1985 Sep;98(3):663–671. doi: 10.1093/oxfordjournals.jbchem.a135323. [DOI] [PubMed] [Google Scholar]
  23. Takano T., Fukuda M., Monma M., Kobayashi S., Kainuma K., Yamane K. Molecular cloning, DNA nucleotide sequencing, and expression in Bacillus subtilis cells of the Bacillus macerans cyclodextrin glucanotransferase gene. J Bacteriol. 1986 Jun;166(3):1118–1122. doi: 10.1128/jb.166.3.1118-1122.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Virolle M. J., Long C. M., Chang S., Bibb M. J. Cloning, characterisation and regulation of an alpha-amylase gene from Streptomyces venezuelae. Gene. 1988 Dec 30;74(2):321–334. doi: 10.1016/0378-1119(88)90166-7. [DOI] [PubMed] [Google Scholar]
  25. Yamazaki H., Ohmura K., Nakayama A., Takeichi Y., Otozai K., Yamasaki M., Tamura G., Yamane K. Alpha-amylase genes (amyR2 and amyE+) from an alpha-amylase-hyperproducing Bacillus subtilis strain: molecular cloning and nucleotide sequences. J Bacteriol. 1983 Oct;156(1):327–337. doi: 10.1128/jb.156.1.327-337.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Yang M., Galizzi A., Henner D. Nucleotide sequence of the amylase gene from Bacillus subtilis. Nucleic Acids Res. 1983 Jan 25;11(2):237–249. doi: 10.1093/nar/11.2.237. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES