Enzyme

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EC Tree
     2. Transferases
        2.4 Glycosyltransferases
            2.4.1 Hexosyltransferases
ID:2.4.1.292
Description:1,4-N-acetyl-D-galactosaminyltransferase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.4.1.292
BRENDA Enzyme Link: BRENDA 2.4.1.292
KEGG Enzyme Link: KEGG2.4.1.292
BioCyc Enzyme Link: BioCyc 2.4.1.292
ExPASy Enzyme Link: ExPASy2.4.1.292
EC2PDB Enzyme Link: EC2PDB 2.4.1.292
ExplorEnz Enzyme Link: ExplorEnz 2.4.1.292
PRIAM enzyme-specific profiles Link: PRIAM 2.4.1.292
IntEnz Enzyme Link: IntEnz 2.4.1.292
MEDLINE Enzyme Link: MEDLINE 2.4.1.292
MSA:

2.4.1.292;

Phylogenetic Tree:

2.4.1.292;

Uniprot:
M-CSA:
RHEA:34519 N-acetyl-alpha-D-galactosaminyl-(1->4)-N-acetyl-alpha-D-galactosaminyl-(1->3)-N,N'-diacetyl-alpha-D-bacillosaminyl-tri-trans,heptacis-undecaprenyl diphosphate + 3 UDP-N-acetyl-alpha-D-galactosamine = [alpha-D-GalNAc-(1->4)]4-alpha-D-GalNAc-(1->3)-alpha-D-diNAcBac-tri-trans,hepta-cis-undecaprenyl diphosphate + 3 H(+) + 3 UDP
RULE(radius=1)
Reaction
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References

TitleAuthorsDatePubMed ID
Genetic and molecular analyses reveal an evolutionary trajectory for glycan synthesis in a bacterial protein glycosylation system.Børud B, Viburiene R, Hartley MD, Paulsen BS, Egge-Jacobsen W, Imperiali B, Koomey M2011 Jun 721606362
Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions.Troutman JM, Imperiali B2009 Mar 3119159314
In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation.Glover KJ, Weerapana E, Imperiali B2005 Oct 416186480