EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
2.4.1.288 | more |
GlfT2 is promiscuous in its substrate preferences. It preferentially acts on substrates in which the lipid-bearing Gal residue is connected to the sequence by a (1->)-beta-glycosidic linkage. The preferential formation of alternating (1->6)-beta-Galf and (1->5)-beta-Galf residues arises not from substrate binding but during catalytic processive polymerization |
Mycobacterium tuberculosis |
? |
- |
- |
2.4.1.288 | more |
among hexoses, monosaccharides, 4-nitrophenyl-furanoses, 4-nitorphenyl-hexoses and disaccharides tested, only methyl alpha-D-mannopyrannoside efficiently reacts as an acceptor. No donor: UDP-alpha-D-glucuronic acid |
Leishmania major |
? |
- |
- |
2.4.1.288 | more |
among hexoses, monosaccharides, 4-nitrophenyl-furanoses, 4-nitorphenyl-hexoses and disaccharides tested, only methyl alpha-D-mannopyrannoside efficiently reacts as an acceptor. No donors: UDP-alpha-D-glucopyranose, UDP-alpha-D-glucuronic acid, GDP-alpha-D-glucopyranose, GDP-alpha-D-mannopyranose |
Leishmania major |
? |
- |
- |
2.4.1.288 | more |
GlfT2 is promiscuous in its substrate preferences. It preferentially acts on substrates in which the lipid-bearing Gal residue is connected to the sequence by a (1->6)-beta-glycosidic linkage. The preferential formation of alternating (1->6)-beta-Galf and (1->5)-beta-Galf residues arises not from substrate binding but during catalytic processive polymerization |
Mycobacterium tuberculosis |
? |
- |
- |
2.4.1.288 | more |
GlfT2 is promiscuous in its substrate preferences. It preferentially acts on substrates in which the lipid-bearing Gal residue is connected to the sequence by a (1->)-beta-glycosidic linkage. The preferential formation of alternating (1->6)-beta-Galf and (1->5)-beta-Galf residues arises not from substrate binding but during catalytic processive polymerization |
Mycobacterium tuberculosis ATCC 25618 |
? |
- |
- |
2.4.1.288 | more |
GlfT2 is promiscuous in its substrate preferences. It preferentially acts on substrates in which the lipid-bearing Gal residue is connected to the sequence by a (1->6)-beta-glycosidic linkage. The preferential formation of alternating (1->6)-beta-Galf and (1->5)-beta-Galf residues arises not from substrate binding but during catalytic processive polymerization |
Mycobacterium tuberculosis ATCC 25618 |
? |
- |
- |
2.4.1.288 | dTDP-alpha-D-galactofuranose + beta-Galf-(1->5)-beta-Galf-(1->6)-beta-Galf-octyl |
- |
Mycobacterium tuberculosis |
UDP + ? |
- |
? |
2.4.1.288 | GDP-alpha-D-glucopyranose + methyl alpha-D-mannopyrannoside |
- |
Leishmania major |
UDP + ? |
- |
? |
2.4.1.288 | GDP-alpha-D-mannopyranose + methyl alpha-D-mannopyrannoside |
- |
Leishmania major |
UDP + ? |
- |
? |
2.4.1.288 | more |
GlfT2 has one active site pocket capable of catalyzing both beta-(1->5) and beta-(1->6) galactofuranosyl transfer reactions |
Mycobacterium tuberculosis |
? |
- |
? |