ID: | 2.4.1.149 |
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Description: | N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase. |
Alternative Name: |
Poly-N-acetyllactosamine extension enzyme. GnTE. acetylglucosaminyltransferase. Beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3- |
Click one PDB to see exact 3D structure provided by NGL.
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 2.4.1.149 |
BRENDA Enzyme Link: | BRENDA 2.4.1.149 |
KEGG Enzyme Link: | KEGG2.4.1.149 |
BioCyc Enzyme Link: | BioCyc 2.4.1.149 |
ExPASy Enzyme Link: | ExPASy2.4.1.149 |
EC2PDB Enzyme Link: | EC2PDB 2.4.1.149 |
ExplorEnz Enzyme Link: | ExplorEnz 2.4.1.149 |
PRIAM enzyme-specific profiles Link: | PRIAM 2.4.1.149 |
IntEnz Enzyme Link: | IntEnz 2.4.1.149 |
MEDLINE Enzyme Link: | MEDLINE 2.4.1.149 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:14389 | a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + UDP-N-acetyl-alpha-D-glucosamine = an N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP |
RULE(radius=1) | [*:1]-[O;H0;+0:2]-[CH;+0:3](-[*:4])-[*:5].[*:6]-[OH;+0:7]>>[*:4]-[CH;+0:3](-[*:5])-[O;H0;+0:7]-[*:6].[*:1]-[OH;+0:2] |
Reaction | ![]() |
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Core-to-Core |
Title | Authors | Date | PubMed ID |
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A beta-1,3-N-acetylglucosaminyltransferase with poly-N-acetyllactosamine synthase activity is structurally related to beta-1,3-galactosyltransferases. | Zhou D, Dinter A, Gutiérrez Gallego R, Kamerling JP, Vliegenthart JF, Berger EG, Hennet T | 1999 Jan 19 | 9892646 |
Novikoff ascites tumor cells contain N-acetyllactosaminide beta 1 leads to 3 and beta 1 leads to 6 N-acetylglucosaminyltransferase activity. | van den Eijnden DH, Winterwerp H, Smeeman P, Schiphorst WE | 1983 Mar 25 | 6219989 |
The presence of N-acetyllactosamine and lactose: beta (1-3)N-acetylglucosaminyltransferase activity in human urine. | Takeya A, Hosomi O, Kogure T | 1985 Feb | 3160874 |
B4GAT1 is the priming enzyme for the LARGE-dependent functional glycosylation of α-dystroglycan. | Praissman JL, Live DH, Wang S, Ramiah A, Chinoy ZS, Boons GJ, Moremen KW, Wells L | 2014 Oct 3 | 25279697 |
Novel sulfated lymphocyte homing receptors and their control by a Core1 extension beta 1,3-N-acetylglucosaminyltransferase. | Yeh JC, Hiraoka N, Petryniak B, Nakayama J, Ellies LG, Rabuka D, Hindsgaul O, Marth JD, Lowe JB, Fukuda M | 2001 Jun 29 | 11439191 |
Identification and characterization of three novel beta 1,3-N-acetylglucosaminyltransferases structurally related to the beta 1,3-galactosyltransferase family. | Shiraishi N, Natsume A, Togayachi A, Endo T, Akashima T, Yamada Y, Imai N, Nakagawa S, Koizumi S, Sekine S, Narimatsu H, Sasaki K | 2001 Feb 2 | 11042166 |