UDP-N-acetylgalactosamine diphosphorylase
(Redirected from UTP:N-acetyl-alpha-D-galactosamine-1-phosphate uridylyltransferase)
| UDP-N-acetylgalactosamine diphosphorylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.83 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
UDP-N-acetylgalactosamine diphosphorylase (EC 2.7.7.83) is an enzyme with systematic name UTP:N-acetyl-alpha-D-galactosamine-1-phosphate uridylyltransferase.[1][2] This enzyme catalyses the following chemical reaction
- UTP + N-acetyl-alpha-D-galactosamine 1-phosphate diphosphate + UDP-N-acetyl-alpha-D-galactosamine
The enzyme from plants and animals also acts on N-acetyl-alpha-D-glucosamine 1-phosphate.
References
[edit]- ^ Wang-Gillam A, Pastuszak I, Elbein AD (October 1998). "A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc". The Journal of Biological Chemistry. 273 (42): 27055–7. doi:10.1074/jbc.273.42.27055. PMID 9765219.
- ^ Peneff C, Ferrari P, Charrier V, Taburet Y, Monnier C, Zamboni V, Winter J, Harnois M, Fassy F, Bourne Y (November 2001). "Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture". The EMBO Journal. 20 (22): 6191–202. doi:10.1093/emboj/20.22.6191. PMC 125729. PMID 11707391.
External links
[edit]- UDP-N-acetylgalactosamine+diphosphorylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
