ID: | 2.4.1.292 |
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Description: | 1,4-N-acetyl-D-galactosaminyltransferase. |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.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: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
Title | Authors | Date | PubMed ID |
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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 M | 2011 Jun 7 | 21606362 |
Campylobacter jejuni PglH is a single active site processive polymerase that utilizes product inhibition to limit sequential glycosyl transfer reactions. | Troutman JM, Imperiali B | 2009 Mar 31 | 19159314 |
In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. | Glover KJ, Weerapana E, Imperiali B | 2005 Oct 4 | 16186480 |