Refine search

Search Reaction

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 8 of 8
EC Number
Reaction
Commentary
Reference
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
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
UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
mechanism
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
-
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
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
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
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
Results 1 - 8 of 8