Structural Investigation and Homology Modeling Studies of Native and Truncated Forms of ![]() |
Ben Abdelmalek, Imen
(Institut National des Sciences Appliquees et de Technologie (INSAT))
Urdaci, Maria Camino (LMBA) Ali, Mamdouh Ben (Centre de Biotechnologie de Sfax) Denayrolles, Muriel (LMBA) Chaignepain, Stephane (Institut Europeen de Chimie et Biologie (IECB)) Limam, Ferid (Institut National des Sciences Appliquees et de Technologie (INSAT)) Bejar, Samir (Centre de Biotechnologie de Sfax) Marzouki, Mohamed Nejib (Institut National des Sciences Appliquees et de Technologie (INSAT)) |
1 |
Ben Abdeimalek Khedher, I., P. Bressollier, M. C. Urdaci, F. Limam, and M. N. Marzouki. 2008. Biochemical characterization of Sclerotinia sclerotiorum |
2 | Benson, D. A., I. Karsch-Mizrachi, D. J. Lipman, J. Ostell, B. A. Rapp, and D. L. Wheeler. 2000. GenBank. Nucleic Acids Res. 28: 15-18 DOI ScienceOn |
3 |
Brzozowski, A. M. and G. J. Davies. 1997. Structure of the Aspergillus oryzae alpha-amylase complexed with the inhibitor acarbose at 2.0 |
4 | Champreda, V., P. Kanokratana, R. Sriprang, S. Tanapongpipat, and L. Eurwilaichitr, 2007. Purification, biochemical characterization, and gene cloning of a new extracellular therrnotolerant and glucose tolerant maltooligosaccharide-forming alpha-amylase from an endophytic ascomycete Fusicoccum sp. BCC4124. Biosci. Biotechnol. Biochem. 71: 2010-2020 DOI ScienceOn |
5 | Ellouze, O., M. Mejri, I. Smaali, F. Limarn, and M. N. Marzouki. 2007. Induction, properties and application of xylanases activity from Sclerotinia sclerotiorum S2 fungus. J. Food Biochem. 31: 96-107 DOI ScienceOn |
6 | Gurr, S. J., S. E. Unkles, and J. R. Kinghoun. 1987. The structure and organization of nuclear genes of filamentous fungi, pp. 93-139. In J. R. Kinghoun (ed.). Gene Structure in Eukaryotic Microbe. IRL Press, Oxford |
7 |
Iefuji, H., M. Chino, M. Kato, and Y. Limura, 1996. Raw starch-digesting and thermostable |
8 |
Janecek, S. 2002. How many conserved sequence regions are there in the |
9 |
Sajedi, R. H., M. Taghdir, H. Naderi-Manesh, K. Khajeh, and B. Ranjbar. 2007. Nucleotide sequence, structural investigation and homology modelling studies of |
10 | Schwed, T., J. Kopp, N. Guex, and M. C. Peitsch. 2003. SWISS-MODEL. An automated protein homology-modeling Server. Nucleic Acid. Res. 31: 3381-3385 DOI ScienceOn |
11 |
Sogaard, M., F. L. Olsen, and B. Svensson. 1991. C-terminal processing of barley |
12 |
Takagi, M., S. Lee, and T. Imanaka. 1996. Diversity in size and alkaliphily of thermostable |
13 | Steyn, A. J., J. Marmur, and I. S. Pretorius. 1995. Cloning, sequence analysis and expression in yeasts of a cDNA containing a Lipomyces kononenkoae alpha-amylase-encoding gene. Gene 166: 65-71 DOI ScienceOn |
14 |
Strobl, S., K. Maskos, M. Betz, G Wiegand, R. Huber, F. X. Gomis-Ruth, and R. Glockshuber. 1998. Crystal structure of yellow meal worm |
15 | Svenssen, B., M. Tovborg Jensen, H. Mori, K. Sass Bak-Jensen, B. Bonsager, P. K. Nielsen, B. Brite Kram hoft, M. Prae torius-Ibba J. Nohr, and N. Juge. 2002. Fascinating facets of function and structure of amylolytic enzyme of glycoside hydrolase family 13. Biologica (Bratislava) 57: 5-19 |
16 | Reymond, P., G. Deleage, C. Rascle, and M. Fevre. 1994. Cloning and sequence analysis of a polygalacturonase-encoding gene from the phytopathogenic fungus Sclerotinia sclerotiorum. Gene 146: 233-237 DOI ScienceOn |
17 |
Kaneko, A., S. Sudo, Y. Takayasu-Sakamoto, G. Tamura, T. Ishikawa, and T. Oba. 1996. Molecular cloning and determination of the nucleotide sequence of a gene encoding an acid-stable |
18 | Wierenga, R K. 2001. The TIM-barrel fold: A versatile framework for efficient enzymes. FEBS Lett. 492: 193-198 DOI PUBMED ScienceOn |
19 |
Ben Ali, M., M. Mezghani, and S. Bejar. 1999. A thermostable |
20 | Jespersen, H. M., E. A. Mac Gregor, M. R. Sierks, and B. Svensson. 1991. Comparison of the domain level organization of starch hydro lases and related enzymes. Biochem. J. 280: 51-55 PUBMED ScienceOn |
21 |
Marco, J. L., L. A. Bataus, F. F. Valencia, C. J. Ulhoa, S. AstolfiFilho, and C. R. Felix. 1996. Purification and characterization of a truncated Bacillus subtilis |
22 |
Swift, H. J., L. Brady, Z. S. Derewanda, E. J. Dodson, G G Dodson, J. P. Turkenburg, and A. J. Wilkinson. 1991. Structure and molecular model refinement of Aspergillus oryzae (TAKA) |
23 |
Boel, E. L., A. M. Brzozowski, Z. Derewenda, G. G. Dodson, V. J. Jensen, S. B. Petersen, H. Swift, L. Thim, and H. F. Woldike. 1990. Calcium binding in |
24 |
MacGregor, E. A, S. Janecek, and B. Svensson. 2001. Relationship of sequence and structure to specificity in the |
25 | Boland, G. J. and R. Hall. 1994. Index of plant hosts of Sclerotinia sclerotiorum. Can. J. Plant Pathol. 16: 94-108 |
26 | Shevchenko, A., M. Wilm, O. Vom, and M. Mann. 1996. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68: 850-858 DOI ScienceOn |
27 | Nakajima, R., T. Imanaka, and S. Aiba. 1985. Comparison of amino acid sequences of eleven different amylase. Appl. Microbiol. Biotechnol. 23: 355-360 ScienceOn |
28 |
Janecek, S., B. Svensson, and B. Henrissat. 1997. Domain evolution in the |
29 | Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTALW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680 DOI ScienceOn |
30 |
Ben Abdeimalek Khedher, I., M. C. Urdaci, F. Limam, M. N. Marzouki, J. M. Schmitter, and P. Bressollier. 2008. Purification, characterization and partial primary sequence of a majormaltotriose-producing |
31 |
Janecek, S. 2000. Structural features and evolutionary relationships in the |
32 | Sanger, F., S. NickIen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. 74: 5463-5467 DOI ScienceOn |
33 | Takasaki, Y., M. Kitaiima, T. Tsuruta, M. Nonoguchi, S. Hayashi, and K. Imada. 1991. Maltotriose-producing amylase from Microbacterium imperiale. Agric. Biol. Chem. 55: 687-692 DOI |
34 | Leemhuis, H., U. F Wehmeier, and L. Dijkhuizen. 2004. Single amino acid mutations interchange the reaction specificities of cyclodextrin glycosyltransferase and the acarbose-modifying enzyme acarviosyl transferase. Biochemistry 43: 13204-13213 DOI ScienceOn |
35 |
Machius, M., G. Wiegand, and R. Huber. 1995. Crystal Structure of Calcium-depleted Bacillus licheniformis |
36 |
Long, C. M., M. J. Virolli, S. Chang, and M. J. Bibb. 1987. Alpha-amylases genes of Streptomyces limosus: Nucleotide sequence, expression motifs and amino acid sequence homology to mammalian and invertebrate |
37 | Miller, G. L. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugars. Anal. Chem. 31: 426-428 DOI |
38 | Birney, E., M. Clamp, and R. Durbin. 2004. Genewise and Genomewise. Genome Res. 14: 988-995 DOI ScienceOn |
39 |
Ohdan, K., T. Kuriki, H. Kaneko, J. Shimada, T. Takada, Z. Fujimoto, H. Mizuno, and S. Okada. 1999. Characteristics of two forms of |
40 | Yoshigi, N., T. Chikano, and M. Kamimura 1985. Characterization of maltopentaose-producing bacterium and its cultural conditions. Agric. Biological Chem. 49: 2379-2384 DOI |
41 | Robyt, J. F. and R. J. Ackerman. 1971. Isolation, purification and characterization of a maltotetraose-producing amylase from Pseudomonas stutzeri. Arch. Biochem. Biophys. 145: 105-114 DOI ScienceOn |
42 | Coutinho, P. M. and B. Henrissat 1999. Carbohydrate-active enzymes: An integrated database approach, pp. 3-12. In H. J. Gilbert, G Davies, B. Henrissat, and B. Svensson (eds.). Recent advances in Carbohydrate Bioengineering. The Royal Society of Chemistry, Cambridge, U.K |
43 | Hayashi, T., T. Akiba, and K. Horikoshi. 1989. Properties of new alkaline maltohexaose forming amylase. Appl. Microbiol. Biotechnol. 28: 281-285 |
44 | Itoh, R., C. Saint-Marc, S. Chaignepain, R. Katahira, J. M. Schmitter, and B. Daignan-Fomier, 2003. The yeast ISNI (YOR155c) gene encodes a new type of IMP-specific 5'-nucleotidase. BMC Biochem. 4: 4-11 DOI PUBMED ScienceOn |
45 |
MacGregor, E. A. 1988. |
46 |
Nielsen, J. E. and T. V. Borchert. 2000. Protein engineering of bacterial |
47 |
Ke, T., X. D. Ma, P. H. Mao, X. Jin, S. J., Chen, Y. Li, L. X. Ma, and G Y. He. 2007. A mutant |
48 |
Matsuura, Y. 2002. A possible mechanism of catalysis involving three essential residues in the enzymes of |
49 |
Van der Maarel, M. J., B. Vander Veen, J. C. Uitdehaag, H. Leemhuis, and L. Dijkhuizen. 2002. Properties and applications of starch converting enzymes of the |
50 |
Vujicic-Zagar, A. and B. W. Dijkstra, 2006. Monoclinic crystal form of Aspergillus niger |
51 | Mandels, M. and J. Webber. 1969. The production of cellulases. Adv. Chem. Ser. 95: 391-412 DOI |
52 |
Brzozowski, A. M., D. M. Lawson, J. P. Turkenburg, H. Bisgaard-Frantzen, A. Svendsen, T. V. Borchert, Z. Dauter, K. S. Wilson, and G. J. Davies. 2000. Structural analysis of a chimeric bacterial |
53 |
Matsubara, T., Y. Ben Ammar, T. Anindyawati, S. Yamamoto, K. Ito, M. lizuka, and N. Minamiura. 2004. Molecular cloning and determination of the nucleotide sequence of raw starch digesting |
54 |
Svenssen, B. 1994. Protein engineering in the |
55 | Nakada, T., M. Kubota, S. Sakari, and Y. Tsujisaka. 1990. Purification and characterization of two forms of maltotetraose-forming amylase from Pseudomonas Stuzeri. Agric. Biol. Chem. 54: 737-743 DOI PUBMED ScienceOn |
56 |
Kim, T. U., B. G. Gu, J. Y. Jeong, S. M. Byurn, and Y. C. Shin. 1995. Purification and characterization of a maltotetraose-forming alkaline |
57 |
Qian, M., R. Haser, G. Buisson, E. Duee, and F. Payan. 1994. The active center of a mammalian |
58 |
Vihinen, M., T. Peltonen, A. Litia, I. Suomien, and P. Mantsata. 1994. C-tenninal truncations of a thermostable Bacillus stearothermophilus |
59 | Kyte, J. and R. Doolittle. 1982. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157: 105-132 DOI PUBMED |
60 | Sambrook, J. E., F. Fritsch, and T. Maniatis. 1989. Molecular Cloning: A laboratory Mammal, New York: Cold Spring Harbor Laboratory Press, New York, U.S.A. |
![]() |