Biology:N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase
| N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.4.1.149 | ||||||||
| CAS number | 85638-39-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase (EC 2.4.1.149) is an enzyme that catalyzes the chemical reaction
- UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R [math]\displaystyle{ \rightleftharpoons }[/math] UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D- glucosaminyl-R
Thus, the two substrates of this enzyme are UDP-N-acetyl-D-glucosamine and beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-R, whereas its 3 products are UDP, N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-D-, and glucosaminyl-R.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-N-acetyl-D-glucosamine:beta-D-galactosyl-1,4-N-acetyl-D-glucosam ine beta-1,3-acetyl-D-glucosaminyltransferase. Other names in common use include uridine diphosphoacetylglucosamine-acetyllactosaminide, beta1->3-acetylglucosaminyltransferase, poly-N-acetyllactosamine extension enzyme, Galbeta1->4GlcNAc-R beta1->3 N-acetylglucosaminyltransferase, UDP-GlcNAc:GalR, beta-D-3-N-acetylglucosaminyltransferase, N-acetyllactosamine beta(1-3)N-acetylglucosaminyltransferase, UDP-GlcNAc:Galbeta1->4GlcNAcbeta-Rbeta1->3-N-, acetylglucosaminyltransferase, and GnTE. This enzyme participates in 4 metabolic pathways: keratan sulfate biosynthesis, glycosphingolipid biosynthesis - neo-lactoseries, glycan structures - biosynthesis 1, and glycan structures - biosynthesis 2.
References
- "The presence of N-acetyllactosamine and lactose: beta (1-3)N-acetylglucosaminyltransferase activity in human urine". Jpn. J. Med. Sci. Biol. 38 (1): 1–8. 1985. doi:10.7883/yoken1952.38.1. PMID 3160874.
- "Novikoff ascites tumor cells contain N-acetyllactosaminide beta 1 leads to 3 and beta 1 leads to 6 N-acetylglucosaminyltransferase activity". J. Biol. Chem. 258 (6): 3435–7. 1983. PMID 6219989.
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