CATH Classification
Domain Context
CATH Clusters
| Superfamily | Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A |
| Functional Family | Beta-1,4-galactosyltransferase 3,4-related |
Enzyme Information
| 2.4.1.90 |
N-acetyllactosamine synthase.
based on mapping to UniProt P15291
UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine.
-!- The reaction is catalyzed by a component of EC 2.4.1.22, which is identical with EC 2.4.1.38, and by an enzyme from the Golgi apparatus of animal tissues. -!- Formerly EC 2.4.1.98.
|
| 2.4.1.- |
Hexosyltransferases.
based on mapping to UniProt P15291
|
| 2.4.1.22 |
Lactose synthase.
based on mapping to UniProt P15291
UDP-alpha-D-galactose + D-glucose = UDP + lactose.
-!- The enzyme is a complex of 2 proteins A and B. -!- In the absence of the B protein (alpha-lactalbumin) the enzyme catalyzes the transfer of galactose from UDP-galactose to N-acetylglucosamine (cf. EC 2.4.1.90).
|
| 2.4.1.38 |
Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase.
based on mapping to UniProt P15291
UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide.
-!- Terminal N-acetyl-beta-D-glucosaminyl residues in polysaccharides, glycoproteins and glycopeptides can act as acceptor. -!- High activity is shown toward such residues in branched-chain polysaccharides when these are linked by beta-1,6 links to galactose residues; lower activity toward residues linked to galactose by beta- 1,3 links. -!- A component of EC 2.4.1.22.
|
UniProtKB Entries (1)
| P15291 |
B4GT1_HUMAN
Homo sapiens
Beta-1,4-galactosyltransferase 1
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PDB Structure
| PDB | 2AE7 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Oligosaccharide Preferences of beta1,4-Galactosyltransferase-I: Crystal Structures of Met340His Mutant of Human beta1,4-Galactosyltransferase-I with a Pentasaccharide and Trisaccharides of the N-Glycan Moiety
J.Mol.Biol.
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