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