Reaction participants Show >> << Hide
- Name help_outline α-Neu5Ac-(2→3)-β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc Identifier CHEBI:145399 Charge -1 Formula C53H87N4O39 InChIKeyhelp_outline PRGHSAXSQGMLMV-RPMMOUILSA-M SMILEShelp_outline [C@@H]1([C@@H]([C@H]([C@H]([C@H](O1)CO)O)O[C@H]2[C@@H]([C@H]([C@@H]([C@H](O2)CO)O[C@H]3[C@@H]([C@H]([C@H]([C@H](O3)CO)O)O[C@]4(O[C@@]([C@@H]([C@H](C4)O)NC(C)=O)([H])[C@@H]([C@@H](CO)O)O)C([O-])=O)O)O)NC(=O)C)O)O[C@H]5[C@@H]([C@H]([C@@H](O[C@@H]5CO)O[C@@H]6[C@H]([C@@H](O[C@@H]([C@@H]6O)CO)O[C@H]7[C@@H]([C@H](C(O[C@@H]7CO)O)NC(=O)C)O)O)NC(=O)C)O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline GDP-β-L-fucose Identifier CHEBI:57273 (Beilstein: 9178112) help_outline Charge -2 Formula C16H23N5O15P2 InChIKeyhelp_outline LQEBEXMHBLQMDB-JGQUBWHWSA-L SMILEShelp_outline C[C@@H]1O[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c2nc(N)[nH]c3=O)[C@@H](O)[C@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 67 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline α-Neu5Ac-(2→3)-β-D-Gal-(1→4)-[α-L-Fuc-(1→3)]-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc-(1→3)-β-D-Gal-(1→4)-β-D-GlcNAc Identifier CHEBI:145398 Charge -1 Formula C59H97N4O43 InChIKeyhelp_outline GHQJUQAWRUPQOF-NTVYDSBRSA-M SMILEShelp_outline [C@@H]1([C@@H]([C@H]([C@H]([C@H](O1)CO)O)O[C@H]2[C@@H]([C@H]([C@@H]([C@H](O2)CO)O[C@H]3[C@@H]([C@H]([C@H]([C@H](O3)CO)O)O[C@]4(O[C@@]([C@@H]([C@H](C4)O)NC(C)=O)([H])[C@@H]([C@@H](CO)O)O)C([O-])=O)O)O[C@H]5[C@H]([C@H](O)[C@@H]([C@H](C)O5)O)O)NC(=O)C)O)O[C@H]6[C@@H]([C@H]([C@@H](O[C@@H]6CO)O[C@@H]7[C@H]([C@@H](O[C@@H]([C@@H]7O)CO)O[C@H]8[C@@H]([C@H](C(O[C@@H]8CO)O)NC(=O)C)O)O)NC(=O)C)O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline GDP Identifier CHEBI:58189 Charge -3 Formula C10H12N5O11P2 InChIKeyhelp_outline QGWNDRXFNXRZMB-UUOKFMHZSA-K SMILEShelp_outline Nc1nc2n(cnc2c(=O)[nH]1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 169 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:62056 | RHEA:62057 | RHEA:62058 | RHEA:62059 | |
---|---|---|---|---|
Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
|
Related reactions help_outline
More general form(s) of this reaction
Publications
-
Complementary acceptor and site specificities of Fuc-TIV and Fuc-TVII allow effective biosynthesis of sialyl-TriLex and related polylactosamines present on glycoprotein counterreceptors of selectins.
Niemelae R., Natunen J., Majuri M.L., Maaheimo H., Helin J., Lowe J.B., Renkonen O., Renkonen R.
The P-selectin counterreceptor PSGL-1 is covalently modified by mono alpha2,3-sialylated, multiply alpha1,3-fucosylated polylactosamines. These glycans are required for the adhesive interactions that allow this adhesion receptor-counterreceptor pair to facilitate leukocyte extravasation. To begin ... >> More
The P-selectin counterreceptor PSGL-1 is covalently modified by mono alpha2,3-sialylated, multiply alpha1,3-fucosylated polylactosamines. These glycans are required for the adhesive interactions that allow this adhesion receptor-counterreceptor pair to facilitate leukocyte extravasation. To begin to understand the biosynthesis of these glycans, we have characterized the acceptor and site specificities of the two granulocyte alpha1,3-fucosyltransferases, Fuc-TIV and Fuc-TVII, using recombinant forms of these two enzymes and a panel of synthetic polylactosamine-based acceptors. We find that Fuc-TIV can transfer fucose effectively to all N-acetyllactosamine (LN) units in neutral polylactosamines, and to the "inner" LN units of alpha2,3-sialylated acceptors but is ineffective in transfer to the distal alpha2,3-sialylated LN unit in alpha2,3-sialylated acceptors. Fuc-TVII, by contrast, effectively fucosylates only the distal alpha2,3-sialylated LN unit in alpha2,3-sialylated acceptors and thus exhibits an acceptor site-specificity that is complementary to Fuc-TIV. Furthermore, the consecutive action of Fuc-TIV and Fuc-TVII, in vitro, can convert the long chain sialoglycan SAalpha2-3'LNbeta1-3'LNbeta1-3'LN (where SA is sialic acid) into the trifucosylated molecule SAalpha2-3'Lexbeta1-3'Lexbeta1-3'Lex (where Lex is the trisaccharide Galbeta1-4(Fucalpha1-3)GlcNAc) known to decorate PSGL-1. The complementary in vitro acceptor site-specificities of Fuc-TIV and Fuc-TVII imply that these enzymes cooperate in vivo in the biosynthesis of monosialylated, multifucosylated polylactosamine components of selectin counterreceptors on human leukocytes. << Less
-
The alpha 1-->3 fucosylation at the penultimate GlcNAc catalyzed by fucosyltransferase VII is blocked by internally fucosylated residue in sialosyl long-chain poly-LacNAc: enzymatic basis for expression of physiological E-selectin epitope.
Handa K., Withers D.A., Hakomori S.
Sialosyl-fucosyl poly-LacNAc without sialosyl-Lex epitope in myeloid cell line HL60 was shown to be the ligand for E-selectin-dependent adhesion, particularly under dynamic flow conditions, in our previous study (Handa K, Stroud MR, Hakomori S, Biochemistry 36, 12412-12420, 1997). HL60 cells expre ... >> More
Sialosyl-fucosyl poly-LacNAc without sialosyl-Lex epitope in myeloid cell line HL60 was shown to be the ligand for E-selectin-dependent adhesion, particularly under dynamic flow conditions, in our previous study (Handa K, Stroud MR, Hakomori S, Biochemistry 36, 12412-12420, 1997). HL60 cells express only fucosyl-transferase (FT) IV and VII. X3NeuAcVII3FucnLc10, a representative component showing E-selectin-dependent binding under dynamic flow conditions, is not alpha 1-->3 fucosylated at the penultimate GlcNAc catalyzed by FT-VII, but is alpha 1-->3 fucosylated at the internal GlcNAc catalyzed by FT-IV. VI3NeuAcnLc6 is converted to VI3NeuAcIII3FucnLc6 by FT-IV, but is also converted to VI3NeuAcV3FucnLc6 by FT-VII. Thus, penultimate fucosylation catalyzed by FT-VII is not restricted for nLc6 backbone, but is highly restricted for nLc10 backbone. The cooperative effect of FT-IV and FT-VII for synthesis of poly-LacNAc having sialosyl-Lex with internal fucosylation may be blocked or highly restricted in poly-LacNAc having more than two LacNAc units, because preferential alpha 1-->3 fucosylation by FT-IV takes place at internal GlcNAc, inhibiting penultimate fucosylation by FT-VII. << Less
Biochem. Biophys. Res. Commun. 243:199-204(1998) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.