From Wikipedia, the free encyclopedia
galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, dimer, Human
Identifiers
EC no. 2.4.1.135
CAS no. 9030-08-4
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
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase ( EC 2.4.1.135) is an enzyme that catalyzes the chemical reaction

UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O- beta-D-xylosylprotein

Thus, the two substrates of this enzyme are UDP-glucuronate and 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein, whereas its 3 products are UDP, 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-, and beta-D-xylosylprotein.

This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucuronate:3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xyl osyl-protein D-glucuronosyltransferase. Other names in common use include glucuronosyltransferase I, and uridine diphosphate glucuronic acid:acceptor glucuronosyltransferase. This enzyme participates in chondroitin sulfate biosynthesis and glycan structures - biosynthesis 1. It employs one cofactor, manganese.

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1V82, 1V83, 1V84, and 2D0J.

References

  • Helting T, Roden L (1969). "Biosynthesis of chondroitin sulfate. II. Glucuronosyl transfer in the formation of the carbohydrate-protein linkage region". J. Biol. Chem. 244 (10): 2799–805. PMID  5770003.
  • Helting T (1972). "Biosynthesis of heparin. Solubilization and partial purification of uridine diphosphate glucuronic acid: acceptor glucuronosyltransferase from mouse mastocytoma". J. Biol. Chem. 247 (13): 4327–32. PMID  4260846.
  • T, Sugahara K; Tone, Y; Tamura, J; Neumann, KW; Ogawa, T; Oka, S; Kawasaki, T; Sugahara, K (1998). "Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans". J. Biol. Chem. 273 (12): 6615–8. doi: 10.1074/jbc.273.12.6615. PMID  9506957.


From Wikipedia, the free encyclopedia
galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, dimer, Human
Identifiers
EC no. 2.4.1.135
CAS no. 9030-08-4
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
Search
PMC articles
PubMed articles
NCBI proteins

In enzymology, a galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase ( EC 2.4.1.135) is an enzyme that catalyzes the chemical reaction

UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O- beta-D-xylosylprotein

Thus, the two substrates of this enzyme are UDP-glucuronate and 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein, whereas its 3 products are UDP, 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O-, and beta-D-xylosylprotein.

This enzyme belongs to the family of glycosyltransferases, specifically the hexosyltransferases. The systematic name of this enzyme class is UDP-glucuronate:3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xyl osyl-protein D-glucuronosyltransferase. Other names in common use include glucuronosyltransferase I, and uridine diphosphate glucuronic acid:acceptor glucuronosyltransferase. This enzyme participates in chondroitin sulfate biosynthesis and glycan structures - biosynthesis 1. It employs one cofactor, manganese.

Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1V82, 1V83, 1V84, and 2D0J.

References

  • Helting T, Roden L (1969). "Biosynthesis of chondroitin sulfate. II. Glucuronosyl transfer in the formation of the carbohydrate-protein linkage region". J. Biol. Chem. 244 (10): 2799–805. PMID  5770003.
  • Helting T (1972). "Biosynthesis of heparin. Solubilization and partial purification of uridine diphosphate glucuronic acid: acceptor glucuronosyltransferase from mouse mastocytoma". J. Biol. Chem. 247 (13): 4327–32. PMID  4260846.
  • T, Sugahara K; Tone, Y; Tamura, J; Neumann, KW; Ogawa, T; Oka, S; Kawasaki, T; Sugahara, K (1998). "Molecular cloning and expression of glucuronyltransferase I involved in the biosynthesis of the glycosaminoglycan-protein linkage region of proteoglycans". J. Biol. Chem. 273 (12): 6615–8. doi: 10.1074/jbc.273.12.6615. PMID  9506957.



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