EC Number   |
Reaction |
Reference |
|---|
   2.4.1.90 | UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine |
catalytic mechanism, enzyme undergoes critical conformational changes upon substrate binding from an open, conf-I, to a closed conformation, conf-II, involving 2 flexible loops, a small and a long one, with Trp314 of the small loop being critical for the change interacting with both substrates, catalytic site structure |
659700 |
| 2.4.1.90 | UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine |
catalytic mechanism, enzyme undergoes critical conformational changes upon substrate binding from an open, conf-I, to a closed conformation, conf-II, involving 2 flexible loops, a small and a long one, with Trp314 of the small loop being critical for the change interacting with both substrates, catalytic site structure, substrate binding structure |
659700 |
| 2.4.1.90 | UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine |
mechanism |
489523 |
| 2.4.1.90 | UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine |
not distinguishable from EC 2.4.1.38 which has identical substrate specificities. EC 2.4.1.38/90 is identical with the A protein of EC 2.4.1.22 |
- |
| 2.4.1.90 | UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine |
sequential ordered catalytic mechanism, enzyme undergoes critical conformational changes upon substrate binding from an open, conf-I, to a closed conformation, conf-II, involving 2 flexible loops, a small and a long one, catalytic site structure, Tyr286 determines the specificity for UDP-Gal |
658502 |
| 2.4.1.90 | UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine |
sequential ordered catalytic mechanism, enzyme undergoes critical conformational changes upon substrate binding from an open, conf-I, to a closed conformation, conf-II, involving 2 flexible loops, a small and a long one, with Trp314 of the small loop being critical for the change interacting with both substrates, catalytic site structure, Tyr289 determines the specificity for UDP-Gal, the conformational changes create the oligosaccharide-acceptor substrate binding site |
658502 |
| 2.4.1.90 | UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine |
the GlcNAc residue at the nonreducing end of chitobiose makes extensive hydrophobic interactions with the highly conserved Tyr286 |
658032 |
| 2.4.1.90 | UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine |
the sequences of cDNA isolated from mammary and F9 cell lines are identical, thus indicating that EC 2.4.1.38 and EC 2.4.1.90 are non-distinguishable |
489496 |
