In enzymology, a N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase (EC 2.4.1.225) is an enzyme that catalyzes the chemical reaction
| N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.4.1.225 | ||||||||
| CAS no. | 145539-84-0 | ||||||||
| 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 | ||||||||
| |||||||||
- UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl- proteoglycan UDP + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)- beta-D-glucuronosyl-proteoglycan
The 3 substrates of this enzyme are UDP-alpha-D-glucuronate, [[N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-]], and proteoglycan, whereas its 3 products are UDP, [[beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-(1->4)-]], and beta-D-glucuronosyl-proteoglycan.
This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-alpha-D-glucuronate:N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D- glucuronosyl-proteoglycan 4-beta-glucuronosyltransferase. Other names in common use include N-acetylglucosaminylproteoglycan beta-1,4-glucuronyltransferase, and heparan glucuronyltransferase II. This enzyme participates in heparan sulfate biosynthesis and glycan structures - biosynthesis 1.
References
edit- K, Lindahl U, Kusche-Gullberg M (2000). "The EXT1/EXT2 tumor suppressors: catalytic activities and role in heparan sulfate biosynthesis". EMBO Reports. 1 (3): 282–6. doi:10.1093/embo-reports/kvd045. PMC 1083719. PMID 11256613.
- Lind T, Tufaro F, McCormick C, Lindahl U, Lidholt K (1998). "The putative tumor suppressors EXT1 and EXT2 are glycosyltransferases required for the biosynthesis of heparan sulfate". J. Biol. Chem. 273 (41): 26265–8. doi:10.1074/jbc.273.41.26265. PMID 9756849.
