Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases
A number of genes encoding bacterial glycosyltransferases have been sequenced during the last few years, but their low sequence similarity has prevented a straightforward grouping of these enzymes into families. The sequences of several bacterial α-mannosyltransferases have been compared using curre...
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| Otros Autores: | , , |
| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
Portland Press Ltd
1996
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
| Aporte de: | Registro referencial: Solicitar el recurso aquí |
| LEADER | 05960caa a22007697a 4500 | ||
|---|---|---|---|
| 001 | PAPER-3520 | ||
| 003 | AR-BaUEN | ||
| 005 | 20230518203259.0 | ||
| 008 | 190411s1996 xx ||||fo|||| 00| 0 eng|d | ||
| 024 | 7 | |2 scopus |a 2-s2.0-0029809688 | |
| 024 | 7 | |2 Molecular Sequence Numbers |a GENBANK: U37258; | |
| 024 | 7 | |2 cas |a glycosyltransferase, 9033-07-2; mannosyltransferase, 9055-06-5 | |
| 040 | |a Scopus |b spa |c AR-BaUEN |d AR-BaUEN | ||
| 030 | |a BIJOA | ||
| 100 | 1 | |a Geremia, R.A. | |
| 245 | 1 | 0 | |a Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases |
| 260 | |b Portland Press Ltd |c 1996 | ||
| 270 | 1 | 0 | |m Henrissat, B.; Ctr Recherches Macromolec Vegetales, Univ Joseph Fourier, CNRS, BP 53, 38041 Grenoble cedex 9, France |
| 506 | |2 openaire |e Política editorial | ||
| 504 | |a Saxena, I.M., Brown, R.M.J., Fèvre, M., Geremia, R.A., Henrissat, B., (1995) J. Bacteriol., 177, pp. 1419-1424 | ||
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| 504 | |a Henrissat, B., (1991) Biochem. J., 280, pp. 309-316 | ||
| 504 | |a Henrissat, B., Bairoch, A., (1993) Biochem. J., 293, pp. 781-788 | ||
| 504 | |a Davies, G., Henrissat, B., (1995) Structure, 3, pp. 853-859 | ||
| 504 | |a Gebler, J., Gilkes, N.R., Claeyssens, M., Wilson, D.B., Béguin, P., Wakarchuk, W.W., Kilburn, D.G., Withers, S.G., (1992) J. Biol. Chem., 267, pp. 12559-12561 | ||
| 504 | |a Paulson, J.C., Colley, K.J., (1989) J. Biol. Chem., 264, pp. 17615-17618 | ||
| 504 | |a Joziasse, D.H., (1992) Glycobiology, 2, pp. 271-277 | ||
| 504 | |a Gaboriaud, C., Bissery, V., Benchetrit, T., Mornon, J.P., (1987) FEBS Lett., 224, pp. 149-155 | ||
| 504 | |a Lemesle-Varloot, L., Henrissat, B., Gaboriaud, C., Bissery, V., Morgat, A., Mornon, J.P., (1990) Biochimie, 72, pp. 555-574 | ||
| 504 | |a Henrissat, B., Callebaut, I., Fabrega, S., Lehn, P., Mornon, J.P., Davies, G., (1995) Proc. Natl. Acad. Sci. U.S.A., 92, pp. 7090-7094 | ||
| 504 | |a Whitfield, C., Valvano, M.A., (1993) Adv. Microb. Physiol., 35, pp. 135-246 | ||
| 504 | |a Liu, D., Haase, A.M., Lindqvist, L., Lindenberg, A.A., Reeves, P.R., (1993) J. Bacteriol., 175, pp. 3408-3413 | ||
| 504 | |a Kido, N., Torgov, V.I., Sugiyama, T., Uchiya, K., Sugihara, H., Komatsu, T., Kato, N., Jann, K., (1995) J. Bacteriol., 177, pp. 2178-2187 | ||
| 504 | |a Capage, M.A., Doherty, D.H., Betlach, M.R., Vanderslice, R.W., (1987), Patent, International Publication Number WO 87/05938; Petroni, E.A., Ielpi, L., (1996) J. Bacteriol., , in the press | ||
| 504 | |a Woodcock, S., Mornon, J.-P., Henrissat, B., (1992) Protein Eng., 5, pp. 629-635 | ||
| 504 | |a Lee, S.J., Romana, L.K., Reeves, P.R., (1992) J. Gen. Microbiol., 138, pp. 1843-1855 | ||
| 504 | |a Miyata, T., Takeda, J., Iida, Y., Yamada, N., Inoue, N., Takahashi, M., Maeda, K., Kinoshita, T., (1993) Science, 259, pp. 1318-1320 | ||
| 504 | |a Schonbachler, M., Horvath, A., Fassler, J., Riezma, H., (1995) EMBO J., 14, pp. 1637-1645 | ||
| 504 | |a Altschul, S.F., Gish, W., Miller, W., Myers, E.W., Lipman, D.J., (1990) J. Mol. Biol., 215, pp. 403-410 | ||
| 520 | 3 | |a A number of genes encoding bacterial glycosyltransferases have been sequenced during the last few years, but their low sequence similarity has prevented a straightforward grouping of these enzymes into families. The sequences of several bacterial α-mannosyltransferases have been compared using current alignment algorithms as well as hydrophobic cluster analysis (HCA). These sequences show a similarity which is significant but too low to be reliably aligned using automatic alignment methods. However, a region spanning approx. 270 residues in these proteins could be aligned by HCA, and several invariant amino acid residues were identified. These features were also found in several other glycosyltransferases, as well as in proteins of unknown function present in sequence databases. This similarity most probably reflects the existence of a family of proteins with conserved structural and mechanistic features. It is argued that the present IUBMB classification of glycosyltransferases could be complemented by a classification of these enzymes based on sequence similarities analogous to that which we proposed for glycosyl hydrolases. |l eng | |
| 593 | |a Centre de Recherches sur les Macromolécules Végétales, Université Joseph Fourier, C.N.R.S., BP 53, 38041 Grenoble Cedex 9, France | ||
| 593 | |a Instituto de Investigaciones Bioquimicas 'Fundacion Campomar', Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Patricias Argentinas 435, (1405) Buenos Aires, Argentina | ||
| 690 | 1 | 0 | |a GLYCOSYLTRANSFERASE |
| 690 | 1 | 0 | |a MANNOSYLTRANSFERASE |
| 690 | 1 | 0 | |a ALGORITHM |
| 690 | 1 | 0 | |a AMINO ACID SEQUENCE |
| 690 | 1 | 0 | |a ARTICLE |
| 690 | 1 | 0 | |a CLUSTER ANALYSIS |
| 690 | 1 | 0 | |a DATA BASE |
| 690 | 1 | 0 | |a GENE SEQUENCE |
| 690 | 1 | 0 | |a NONHUMAN |
| 690 | 1 | 0 | |a PRIORITY JOURNAL |
| 690 | 1 | 0 | |a PROTEIN FAMILY |
| 690 | 1 | 0 | |a BACTERIA (MICROORGANISMS) |
| 690 | 1 | 0 | |a PROKARYOTA |
| 700 | 1 | |a Petroni, E.A. | |
| 700 | 1 | |a Ielpi, L. | |
| 700 | 1 | |a Henrissat, B. | |
| 773 | 0 | |d Portland Press Ltd, 1996 |g v. 318 |h pp. 133-138 |k n. 1 |p BIOCHEM. J. |x 02646021 |w (AR-BaUEN)CENRE-205 |t Biochemical Journal | |
| 856 | 4 | 1 | |u https://www.scopus.com/inward/record.uri?eid=2-s2.0-0029809688&doi=10.1042%2fbj3180133&partnerID=40&md5=53cffaf6e85993458bbd0514d666f6ad |y Registro en Scopus |
| 856 | 4 | 0 | |u https://doi.org/10.1042/bj3180133 |y DOI |
| 856 | 4 | 0 | |u https://hdl.handle.net/20.500.12110/paper_02646021_v318_n1_p133_Geremia |y Handle |
| 856 | 4 | 0 | |u https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02646021_v318_n1_p133_Geremia |y Registro en la Biblioteca Digital |
| 961 | |a paper_02646021_v318_n1_p133_Geremia |b paper |c PE | ||
| 962 | |a info:eu-repo/semantics/article |a info:ar-repo/semantics/artículo |b info:eu-repo/semantics/publishedVersion | ||
| 963 | |a VARI | ||
| 999 | |c 64473 | ||