Probing the substrate specificity of four different sialyltransferases using synthetic beta-D-Galp-(1-->4)-beta-D-GlcpNAc-(1-->2)-alpha-D-Manp-(1-->O) (CH(2))7CH3 analogues general activating effect of replacing N-acetylglucosamine by N-propionylglucosamine.
| Autoři: | Rohfritsch PF; Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht University, Padualaan 8, NL-3584 CH Utrecht, The Netherlands., Joosten JA, Krzewinski-Recchi MA, Harduin-Lepers A, Laporte B, Juliant S, Cerutti M, Delannoy P, Vliegenthart JF, Kamerling JP |
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| Zdroj: | Biochimica et biophysica acta [Biochim Biophys Acta] 2006 Apr; Vol. 1760 (4), pp. 685-92. Date of Electronic Publication: 2006 Jan 06. |
| Způsob vydávání: | Journal Article; Research Support, Non-U.S. Gov't |
| Jazyk: | English |
| Informace o časopise: | Publisher: Elsevier Pub. Co Country of Publication: Netherlands NLM ID: 0217513 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0006-3002 (Print) Linking ISSN: 00063002 NLM ISO Abbreviation: Biochim Biophys Acta Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: Amsterdam : Elsevier Pub. Co. |
| Výrazy ze slovníku MeSH: | Oligosaccharides/*metabolism , Sialyltransferases/*metabolism, Acetylglucosamine ; Animals ; Carbohydrate Sequence ; Glucosamine/analogs & derivatives ; Humans ; Oligosaccharides/chemistry ; Rats ; Structure-Activity Relationship ; Substrate Specificity |
| Abstrakt: | The acceptor specificities of ST3Gal III, ST3Gal IV, ST6Gal I and ST6Gal II were investigated using a panel of beta-D-Galp-(1-->4)-beta-D-GlcpNAc-(1-->2)-alpha-D-Manp-(1-->O)(CH(2))(7)CH(3) analogues. Modifications introduced at either C2, C3, C4, C5, or C6 of terminal D-Gal, as well as N-propionylation instead of N-acetylation of subterminal D-GlcN were tested for their influence on the alpha-2,3- and alpha-2,6-sialyltransferase acceptor activities. Both ST3Gal enzymes displayed the same narrow acceptor specificity, and only accept reduction of the Gal C2 hydroxyl function. The ST6Gal enzymes, however, do not have the same acceptor specificity. ST6Gal II seems less tolerant towards modifications at Gal C3 and C4 than ST6Gal I, and prefers beta-D-GalpNAc-(1-->4)-beta-D-GlcpNAc (LacdiNAc) as an acceptor substrate, as shown by replacing the Gal C2 hydroxyl group with an N-acetyl function. Finally, a particularly striking feature of all tested sialyltransferases is the activating effect of replacing the N-acetyl function of subterminal GlcNAc by an N-propionyl function. |
| Substance Nomenclature: | 0 (Oligosaccharides) 40549-20-0 (N-propanoylglucosamine) EC 2.4.99.- (Sialyltransferases) N08U5BOQ1K (Glucosamine) V956696549 (Acetylglucosamine) |
| Entry Date(s): | Date Created: 20060128 Date Completed: 20060609 Latest Revision: 20161126 |
| Update Code: | 20221213 |
| DOI: | 10.1016/j.bbagen.2005.12.012 |
| PMID: | 16439063 |
| Autor: | Rohfritsch PF; Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht University, Padualaan 8, NL-3584 CH Utrecht, The Netherlands., Joosten JA, Krzewinski-Recchi MA, Harduin-Lepers A, Laporte B, Juliant S, Cerutti M, Delannoy P, Vliegenthart JF, Kamerling JP |
| Jazyk: | angličtina |
| Zdroj: | Biochimica et biophysica acta [Biochim Biophys Acta] 2006 Apr; Vol. 1760 (4), pp. 685-92. Date of Electronic Publication: 2006 Jan 06. |
| DOI: | 10.1016/j.bbagen.2005.12.012 |
| Abstrakt: | The acceptor specificities of ST3Gal III, ST3Gal IV, ST6Gal I and ST6Gal II were investigated using a panel of beta-D-Galp-(1-->4)-beta-D-GlcpNAc-(1-->2)-alpha-D-Manp-(1-->O)(CH(2))(7)CH(3) analogues. Modifications introduced at either C2, C3, C4, C5, or C6 of terminal D-Gal, as well as N-propionylation instead of N-acetylation of subterminal D-GlcN were tested for their influence on the alpha-2,3- and alpha-2,6-sialyltransferase acceptor activities. Both ST3Gal enzymes displayed the same narrow acceptor specificity, and only accept reduction of the Gal C2 hydroxyl function. The ST6Gal enzymes, however, do not have the same acceptor specificity. ST6Gal II seems less tolerant towards modifications at Gal C3 and C4 than ST6Gal I, and prefers beta-D-GalpNAc-(1-->4)-beta-D-GlcpNAc (LacdiNAc) as an acceptor substrate, as shown by replacing the Gal C2 hydroxyl group with an N-acetyl function. Finally, a particularly striking feature of all tested sialyltransferases is the activating effect of replacing the N-acetyl function of subterminal GlcNAc by an N-propionyl function. |
| Databáze: | MEDLINE |
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