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1860799823731490816
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INTELEK Repository
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| collection |
Online Access
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| collectionurl |
https://intelek.unisza.edu.my/intelek/pages/search.php?search=!collection407072
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| date |
2011-07-18 14:54:57
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| format |
Restricted Document
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| id |
7537
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UniSZA
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Alias, N., Mahadi, N. M., Abdul Murad, A. M., Abu Bakar, F. D., Nik Mahmood, N. A. & Md Illias, R. 2009. Expression and characterization of Trichoderma virens UKM-1 endochitinase in Escherichia coli. World Journal of Microbiology and Biotechnology 25: 561-572. Boer, H., Simolin, H., Cottaz, S., Söderlund, H. & Koivula, A. 2007. Heterologous expression and site-directed mutagenesis studies of two Trichoderma harzianum chitinases, Chit33 and Chit42, in Escherichia coli. Protein Expression and Purification 51: 216-226. Brurberg, M, B., Synstad, B., Klemsdal, S. S., van Aalten, D. M. F., Sundheim, L. & Eijsink, G. H. 2000. Chitinases from Serratia marcescens. Manuscript Recent Research Developments in Microbiology. p. 1-18. Fukamizo, T. 2000. Chitinolytic enzymes: Catalysis, substrate binding, and their application. Current Protein and Peptide Science 1: 105-124. Gooday, G. W. 1994. Biochemistry of Microbial Degradation. Dordecht, Netherlands: Kluwer. p. 279-312. Gustav, V. K., Houston, D. R., Rao, F. V., Peter, M. G., Synstad, B., van Aalten D. M. F. & Eijsink, V. G. H. 2004. Structure of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidin. Biochimica et Biophysica Acta 1696: 103-111. Hayes, C. K., Klemsdal, S., Lorito, M., Di Pietro, A., Peterbauer, C., Nakas, J. P., Tronsmo, A. & Harman, G. E. 1994. Isolation and sequence of an endochitinase-encoding gene from cDNA library of Trichoderma harzianum. Gene 138: 143-148. Hahm, D. H., Kim, S. H., Pan, J. & Rhee, J. S. 1995. Maximum yield of foreign lipase in Escherichia coli HB101 limited by duration of protein expression. Journal of Fermentation and Bioengineering 79(3): 236-241. Hart, P. J., Pfluger, H. D., Monzingo, A. F., Hollis, T. & Robertus, J. D. 1995. The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 Å resolution. Journal of Molecular Biology 248: 402-413. Hollis, T., Monzingo, A. F., Bortone, K., Ernst, S., Cox, R. & Robertus, J. D. 2000. The X-ray structure of a chitinase from the pathogenic fungus Coccidiodes immitis. Protein Science 9: 544-551. Ikegami, T., Okada, T., Hashimoto, M., Seino, S., Watanabe, T. & Shirakawa, M. 2000. Solution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1. The Journal of Biological Chemistry 275(18): 13654-13661. Kim, D. J., Baek, J. M., Uribe, P., Kenerley, C. M. & Cook, D. R. 2002. Cloning and characterization of multiple glycosyl hydrolase genes from Trichoderma virens. Current Genetics 40: 374-384. Lin, T. Y. & Koshland, D. E., Jr. 1969. Carboxyl group modification and the activity of lysozyme. The Journal of Biological Chemistry 244(2): 505–508. Malcolm, B. A, Rosenberg, S., Corey, M. J., Allen, J. S., de Baetselier, A. & Kirsch, J. F. 1989. Site�directed mutagenesis of the catalytic residues Asp-52 and Glu-35 of chicken egg white lysozyme. Proceedings of the National Academy of Sciences USA 86: 133-137. Matsumoto, T., Nonaka, T., Hashimoto, M., Watanabe, T. & Mitsui, Y. 1999. Three-dimensional structure of the catalytic domain of chitinase A1 from Bacillus circulans WL-12 at a very high resolution. Proceedings of the Japan Academy 75: 269-274. Mononen, I. & Karjalainen, E. 1984. Structural comparison of protein sequences around potential N-glycosylation sites. Biochimica Biophysica Acta 788: 364-367. Patil, R. S., Ghormade, V. & Deshpande, M. V. 2000. Chitinolytic enzymes: An exploration. Enzyme and Microbial Technology 26: 473-483. Ueda, M., Okada, A., Kawaguchi, T. & Arai, M. 1998. Cloning and sequence analysis of a chitinase gene (pCA8 ORF) from Aeromonas sp. no. 10S-24. Journal of Fermentation and Bioengineering 86(6): 600-604. Van Aalten, D. M. F., Synstad, B., Brurberg, M. B., Hough, E., Riise, B. W., Eijsink, V. G. H. & Wierenga, R. K. 2000. Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9 Å resolution. Proceeding of the National Academy of Sciences USA 97: 5842-5847. Van Scheltinga, A. C. T., Kalk, K. H., Beintema, J. J. & Dijkstra, B. W. 1994. Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor. Structure 2: 1181–1189. Van Scheltinga, A. C. T., Hennig, M. & Dijkstra, B. W. 1996. The 1.8 Å resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18. Journal of Molecular Biology 262: 243-257. Watanabe, T., Kobori, K., Miyashita, K., Fujii, T., Sakai, H., Uchida, M. & Tanaka, H. 1993. Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. Journal of Biological Chemistry 268: 18567- 18572. Zhang, R. 1999. Chitinases in Serratia marcescens: A representative of family 18 chitinases. Report for Advance Biochemistry and Molecular Biology. p. 1-18.
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3078-01-FH02-FPBSM-14-00885.pdf
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7537 https://intelek.unisza.edu.my/intelek/pages/view.php?ref=7537 https://intelek.unisza.edu.my/intelek/pages/search.php?search=!collection407072 Restricted Document Article Journal application/pdf 10 1.6 Adobe Acrobat Pro DC 20 Paper Capture Plug-in Adobe InDesign CS5 (7.0) xmp.did:F77F1174072068118A6DDA55DAEB057D 2011-07-18 14:54:57 3078-01-FH02-FPBSM-14-00885.pdf UniSZA Private Access Three Dimensional Structure Prediction of Recombinant Endochitinase from Trichoderma virens UKM-1 Three Dimensional Structure Prediction of Recombinant Endochitinase from Trichoderma virens UKM-1 Chitinases (EC 3.2.11.14) are capable of hydrolyzing chitins by splitting their ß-1,4-glucosidic bonds. They are present in a wide range of organisms including the fungus Trichoderma virens UKM-1. A gene encoding endochitinase from Trichoderma virens UKM-1 had successfully been cloned (with GenBank Accession number DQ 865246) and expressed in Escherichia coli BL21 (DE3). As a member of glycosyl hydrolases, chitinases are assumed to have a similar catalytic mechanism and structure as other enzymes such as lysozyme. A predicted three dimensional (3D) structure of endochitinase derived from Trichoderma virens UKM-1 was successfully constructed using the Swiss-Prot model server and analyzed by PyMOL software. The prediction of the structure was done by comparing T. virens UKM-1 endochitinase with seven published 3D structures of chitinases from the Swiss-Prot database. Recombinant endochitinase from T. virens UKM-1 was shown to have a TIM-barrel structure with eight parallel ß-sheets and eight α-helices laid down in the inner barrel together with three-stranded ß-sheets. These characteristics revealed the aspects of the catalytic centers of family 18 chitinases. An extensive study was done on the multiple sequence alignment of various class V, family 18 chitinases by using DNASIS Software. Two conserved consensus motif boxes SxGG (Box 1) and DxxDxDxE (Box 2) were found at the N-terminal amino acid sequence of endochitinase from T. virens UKM-1 which were involved in catalysis. 2 83-92 Alias, N., Mahadi, N. M., Abdul Murad, A. M., Abu Bakar, F. D., Nik Mahmood, N. A. & Md Illias, R. 2009. Expression and characterization of Trichoderma virens UKM-1 endochitinase in Escherichia coli. World Journal of Microbiology and Biotechnology 25: 561-572. Boer, H., Simolin, H., Cottaz, S., Söderlund, H. & Koivula, A. 2007. Heterologous expression and site-directed mutagenesis studies of two Trichoderma harzianum chitinases, Chit33 and Chit42, in Escherichia coli. Protein Expression and Purification 51: 216-226. Brurberg, M, B., Synstad, B., Klemsdal, S. S., van Aalten, D. M. F., Sundheim, L. & Eijsink, G. H. 2000. Chitinases from Serratia marcescens. Manuscript Recent Research Developments in Microbiology. p. 1-18. Fukamizo, T. 2000. Chitinolytic enzymes: Catalysis, substrate binding, and their application. Current Protein and Peptide Science 1: 105-124. Gooday, G. W. 1994. Biochemistry of Microbial Degradation. Dordecht, Netherlands: Kluwer. p. 279-312. Gustav, V. K., Houston, D. R., Rao, F. V., Peter, M. G., Synstad, B., van Aalten D. M. F. & Eijsink, V. G. H. 2004. Structure of the D142N mutant of the family 18 chitinase ChiB from Serratia marcescens and its complex with allosamidin. Biochimica et Biophysica Acta 1696: 103-111. Hayes, C. K., Klemsdal, S., Lorito, M., Di Pietro, A., Peterbauer, C., Nakas, J. P., Tronsmo, A. & Harman, G. E. 1994. Isolation and sequence of an endochitinase-encoding gene from cDNA library of Trichoderma harzianum. Gene 138: 143-148. Hahm, D. H., Kim, S. H., Pan, J. & Rhee, J. S. 1995. Maximum yield of foreign lipase in Escherichia coli HB101 limited by duration of protein expression. Journal of Fermentation and Bioengineering 79(3): 236-241. Hart, P. J., Pfluger, H. D., Monzingo, A. F., Hollis, T. & Robertus, J. D. 1995. The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 Å resolution. Journal of Molecular Biology 248: 402-413. Hollis, T., Monzingo, A. F., Bortone, K., Ernst, S., Cox, R. & Robertus, J. D. 2000. The X-ray structure of a chitinase from the pathogenic fungus Coccidiodes immitis. Protein Science 9: 544-551. Ikegami, T., Okada, T., Hashimoto, M., Seino, S., Watanabe, T. & Shirakawa, M. 2000. Solution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1. The Journal of Biological Chemistry 275(18): 13654-13661. Kim, D. J., Baek, J. M., Uribe, P., Kenerley, C. M. & Cook, D. R. 2002. Cloning and characterization of multiple glycosyl hydrolase genes from Trichoderma virens. Current Genetics 40: 374-384. Lin, T. Y. & Koshland, D. E., Jr. 1969. Carboxyl group modification and the activity of lysozyme. The Journal of Biological Chemistry 244(2): 505–508. Malcolm, B. A, Rosenberg, S., Corey, M. J., Allen, J. S., de Baetselier, A. & Kirsch, J. F. 1989. Site�directed mutagenesis of the catalytic residues Asp-52 and Glu-35 of chicken egg white lysozyme. Proceedings of the National Academy of Sciences USA 86: 133-137. Matsumoto, T., Nonaka, T., Hashimoto, M., Watanabe, T. & Mitsui, Y. 1999. Three-dimensional structure of the catalytic domain of chitinase A1 from Bacillus circulans WL-12 at a very high resolution. Proceedings of the Japan Academy 75: 269-274. Mononen, I. & Karjalainen, E. 1984. Structural comparison of protein sequences around potential N-glycosylation sites. Biochimica Biophysica Acta 788: 364-367. Patil, R. S., Ghormade, V. & Deshpande, M. V. 2000. Chitinolytic enzymes: An exploration. Enzyme and Microbial Technology 26: 473-483. Ueda, M., Okada, A., Kawaguchi, T. & Arai, M. 1998. Cloning and sequence analysis of a chitinase gene (pCA8 ORF) from Aeromonas sp. no. 10S-24. Journal of Fermentation and Bioengineering 86(6): 600-604. Van Aalten, D. M. F., Synstad, B., Brurberg, M. B., Hough, E., Riise, B. W., Eijsink, V. G. H. & Wierenga, R. K. 2000. Structure of a two-domain chitotriosidase from Serratia marcescens at 1.9 Å resolution. Proceeding of the National Academy of Sciences USA 97: 5842-5847. Van Scheltinga, A. C. T., Kalk, K. H., Beintema, J. J. & Dijkstra, B. W. 1994. Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor. Structure 2: 1181–1189. Van Scheltinga, A. C. T., Hennig, M. & Dijkstra, B. W. 1996. The 1.8 Å resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18. Journal of Molecular Biology 262: 243-257. Watanabe, T., Kobori, K., Miyashita, K., Fujii, T., Sakai, H., Uchida, M. & Tanaka, H. 1993. Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. Journal of Biological Chemistry 268: 18567- 18572. Zhang, R. 1999. Chitinases in Serratia marcescens: A representative of family 18 chitinases. Report for Advance Biochemistry and Molecular Biology. p. 1-18.
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| spellingShingle |
Three Dimensional Structure Prediction of Recombinant Endochitinase from Trichoderma virens UKM-1
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| summary |
Chitinases (EC 3.2.11.14) are capable of hydrolyzing chitins by splitting their ß-1,4-glucosidic bonds. They are present in a wide range of organisms including the fungus Trichoderma virens UKM-1. A gene encoding endochitinase from Trichoderma virens UKM-1 had successfully been cloned (with GenBank Accession number DQ 865246) and expressed in Escherichia coli BL21 (DE3). As a member of glycosyl hydrolases, chitinases are assumed to have a similar catalytic mechanism and structure as other enzymes such as lysozyme. A predicted three dimensional (3D) structure of endochitinase derived from Trichoderma virens UKM-1 was successfully constructed using the Swiss-Prot model server and analyzed by PyMOL software. The prediction of the structure was done by comparing T. virens UKM-1 endochitinase with seven published 3D structures of chitinases from the Swiss-Prot database. Recombinant endochitinase from T. virens UKM-1 was shown to have a TIM-barrel structure with eight parallel ß-sheets and eight α-helices laid down in the inner barrel together with three-stranded ß-sheets. These characteristics revealed the aspects of the catalytic centers of family 18 chitinases. An extensive study was done on the multiple sequence alignment of various class V, family 18 chitinases by using DNASIS Software. Two conserved consensus motif boxes SxGG (Box 1) and DxxDxDxE (Box 2) were found at the N-terminal amino acid sequence of endochitinase from T. virens UKM-1 which were involved in catalysis.
|
| title |
Three Dimensional Structure Prediction of Recombinant Endochitinase from Trichoderma virens UKM-1
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| title_full |
Three Dimensional Structure Prediction of Recombinant Endochitinase from Trichoderma virens UKM-1
|
| title_fullStr |
Three Dimensional Structure Prediction of Recombinant Endochitinase from Trichoderma virens UKM-1
|
| title_full_unstemmed |
Three Dimensional Structure Prediction of Recombinant Endochitinase from Trichoderma virens UKM-1
|
| title_short |
Three Dimensional Structure Prediction of Recombinant Endochitinase from Trichoderma virens UKM-1
|
| title_sort |
three dimensional structure prediction of recombinant endochitinase from trichoderma virens ukm-1
|