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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1996
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02646021_v318_n1_p133_Geremia http://hdl.handle.net/20.500.12110/paper_02646021_v318_n1_p133_Geremia |
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paper:paper_02646021_v318_n1_p133_Geremia2023-06-08T15:23:09Z Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases Geremía, Roberto Alejandro Petroni, Eberto Alejandro Ielpi, Luis glycosyltransferase mannosyltransferase algorithm amino acid sequence article cluster analysis data base gene sequence nonhuman priority journal protein family Bacteria (microorganisms) Prokaryota 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. Fil:Geremia, R.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Petroni, E.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Ielpi, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1996 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02646021_v318_n1_p133_Geremia http://hdl.handle.net/20.500.12110/paper_02646021_v318_n1_p133_Geremia |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
glycosyltransferase mannosyltransferase algorithm amino acid sequence article cluster analysis data base gene sequence nonhuman priority journal protein family Bacteria (microorganisms) Prokaryota |
| spellingShingle |
glycosyltransferase mannosyltransferase algorithm amino acid sequence article cluster analysis data base gene sequence nonhuman priority journal protein family Bacteria (microorganisms) Prokaryota Geremía, Roberto Alejandro Petroni, Eberto Alejandro Ielpi, Luis Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases |
| topic_facet |
glycosyltransferase mannosyltransferase algorithm amino acid sequence article cluster analysis data base gene sequence nonhuman priority journal protein family Bacteria (microorganisms) Prokaryota |
| description |
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. |
| author |
Geremía, Roberto Alejandro Petroni, Eberto Alejandro Ielpi, Luis |
| author_facet |
Geremía, Roberto Alejandro Petroni, Eberto Alejandro Ielpi, Luis |
| author_sort |
Geremía, Roberto Alejandro |
| title |
Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases |
| title_short |
Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases |
| title_full |
Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases |
| title_fullStr |
Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases |
| title_full_unstemmed |
Towards a classification of glycosyltransferases based on amino acid sequence similarities: Prokaryotic α-mannosyltransferases |
| title_sort |
towards a classification of glycosyltransferases based on amino acid sequence similarities: prokaryotic α-mannosyltransferases |
| publishDate |
1996 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_02646021_v318_n1_p133_Geremia http://hdl.handle.net/20.500.12110/paper_02646021_v318_n1_p133_Geremia |
| work_keys_str_mv |
AT geremiarobertoalejandro towardsaclassificationofglycosyltransferasesbasedonaminoacidsequencesimilaritiesprokaryoticamannosyltransferases AT petroniebertoalejandro towardsaclassificationofglycosyltransferasesbasedonaminoacidsequencesimilaritiesprokaryoticamannosyltransferases AT ielpiluis towardsaclassificationofglycosyltransferasesbasedonaminoacidsequencesimilaritiesprokaryoticamannosyltransferases |
| _version_ |
1768542985196142592 |