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Literature summary extracted from

  • Liu, T.W.; Kaji, H.; Togayachi, A.; Ito, H.; Sato, T.; Narimatsu, H.
    A chemoenzymatic approach toward the identification of fucosylated glycoproteins and mapping of N-glycan sites (2012), Glycobiology, 22, 630-637.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.7.1.52 analysis development of an alternative way of labeling of fucosylated structures by metabolic engineering for the identification of fucosylated glycoproteins, using a chemoenzymatic approach. In this approach, the activities of Bacteroides fragilis 9343 L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase and human alpha1,3-fucosyltransferase 9 are combined in a Namalwa cellular model, the system can be applied to labeling of alkyne-modified fucosylated glycoproteins, e.g. for labeling of alkynyl fucose containing glycans, N-linked glycosylation site mapping and fucosylated glycoprotein identification by IGOT-LC-MS analysis, overview Bacteroides fragilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.52 Mg2+ required Bacteroides fragilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.52 ATP + L-fucose Bacteroides fragilis
-
 ADP + beta-L-fucose 1-phosphate
-
 ?
2.7.1.52 ATP + L-fucose Bacteroides fragilis 9343
-
 ADP + beta-L-fucose 1-phosphate
-
 ?
2.7.1.52 additional information Bacteroides fragilis development of an alternative way of labeling of fucosylated structures by metabolic engineering for the identification of fucosylated glycoproteins, using a chemoenzymatic approach. In this approach, the activities of Bacteroides fragilis 9343 L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase and human alpha1,3-fucosyltransferase 9 are combined in a Namalwa cellular model, the system can be applied to labeling of alkyne-modified fucosylated glycoproteins, e.g. for labeling of alkynyl fucose containing glycans, N-linked glycosylation site mapping and fucosylated glycoprotein identification by IGOT-LC-MS analysis, overview ?
-
 ?
2.7.1.52 additional information Bacteroides fragilis 9343 development of an alternative way of labeling of fucosylated structures by metabolic engineering for the identification of fucosylated glycoproteins, using a chemoenzymatic approach. In this approach, the activities of Bacteroides fragilis 9343 L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase and human alpha1,3-fucosyltransferase 9 are combined in a Namalwa cellular model, the system can be applied to labeling of alkyne-modified fucosylated glycoproteins, e.g. for labeling of alkynyl fucose containing glycans, N-linked glycosylation site mapping and fucosylated glycoprotein identification by IGOT-LC-MS analysis, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.214 Homo sapiens
-
-
-
2.7.1.52 Bacteroides fragilis
-
-
-
2.7.1.52 Bacteroides fragilis 9343
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.214 NAMALWA cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.52 ATP + L-fucose
-
 Bacteroides fragilis ADP + beta-L-fucose 1-phosphate
-
 ?
2.7.1.52 ATP + L-fucose
-
 Bacteroides fragilis 9343 ADP + beta-L-fucose 1-phosphate
-
 ?
2.7.1.52 additional information development of an alternative way of labeling of fucosylated structures by metabolic engineering for the identification of fucosylated glycoproteins, using a chemoenzymatic approach. In this approach, the activities of Bacteroides fragilis 9343 L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase and human alpha1,3-fucosyltransferase 9 are combined in a Namalwa cellular model, the system can be applied to labeling of alkyne-modified fucosylated glycoproteins, e.g. for labeling of alkynyl fucose containing glycans, N-linked glycosylation site mapping and fucosylated glycoprotein identification by IGOT-LC-MS analysis, overview Bacteroides fragilis ?
-
 ?
2.7.1.52 additional information development of an alternative way of labeling of fucosylated structures by metabolic engineering for the identification of fucosylated glycoproteins, using a chemoenzymatic approach. In this approach, the activities of Bacteroides fragilis 9343 L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase and human alpha1,3-fucosyltransferase 9 are combined in a Namalwa cellular model, the system can be applied to labeling of alkyne-modified fucosylated glycoproteins, e.g. for labeling of alkynyl fucose containing glycans, N-linked glycosylation site mapping and fucosylated glycoprotein identification by IGOT-LC-MS analysis, overview Bacteroides fragilis 9343 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.214 alpha1,3-fucosyltransferase 9
-
 Homo sapiens
2.4.1.214 Fut9
-
 Homo sapiens
2.7.1.52 FKP
-
 Bacteroides fragilis
2.7.1.52 L-fucokinase/guanosine 5'-diphosphate-L-fucose pyrophosphorylase
-
 Bacteroides fragilis
2.7.1.52 L-fucokinase/guanosine-5'-diphosphate-Fuc pyrophosphorylase
-
 Bacteroides fragilis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.52 ATP
-
 Bacteroides fragilis

General Information

EC Number General Information Comment Organism
2.7.1.52 metabolism the enzyme catalyzes the first step of the salvage pathway converting exogenous L-Fuc to GDP-L-Fuc Bacteroides fragilis
2.7.1.52 physiological function the bifunctional L-Fuc pyrophosphorylase, FKP, converts L-Fuc into GDP-L-Fuc via an L-Fuc-1-phosphate intermediate Bacteroides fragilis