UTP:galactose-1-phosphate uridylyltransferase | |||||||||
---|---|---|---|---|---|---|---|---|---|
UTP—galactose-1-phosphate uridylyltransferase homodimer, E.Coli | |||||||||
Identifiers | |||||||||
EC no. | 2.7.7.10 | ||||||||
CAS no. | 9016-11-9 | ||||||||
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 | ||||||||
|
In enzymology, an UTP—hexose-1-phosphate uridylyltransferase (EC 2.7.7.10) is an enzyme that catalyzes the chemical reaction
- UTP + alpha-D-galactose 1-phosphate diphosphate + UDP-galactose
Thus, the two substrates of this enzyme are UTP and alpha-D-galactose 1-phosphate, whereas its two products are diphosphate and UDP-galactose.
Enzyme family
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is UTP:alpha-D-hexose-1-phosphate uridylyltransferase. Other names in common use include galactose-1-phosphate uridylyltransferase, galactose 1-phosphate uridylyltransferase, alpha-D-galactose 1-phosphate uridylyltransferase, galactose 1-phosphate uridyltransferase, UDPgalactose pyrophosphorylase, uridine diphosphate galactose pyrophosphorylase, and uridine diphosphogalactose pyrophosphorylase. This enzyme participates in galactose metabolism and nucleotide sugars metabolism.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1GUP, 1GUQ, and 1HXP.
References
- ISSELBACHER KJ (1958). "A mammalian uridinediphosphate galactose pyrophosphorylase". J. Biol. Chem. 232 (1): 429–44. doi:10.1016/S0021-9258(18)70408-0. PMID 13549431.
- KALCKAR HM (1953). "The role of phosphoglycosyl compounds in the biosynthesis of nucleosides and nucleotides". Biochim. Biophys. Acta. 12 (1–2): 250–64. doi:10.1016/0006-3002(53)90144-9. PMID 13115434.
- Lee L, Kimura A, Tochikura T (October 1979). "Purification and properties of UDP-glucose (UDP-galactose) pyrophosphorylase from Bifidobacterium bifidum". J. Biochem. 86 (4). Tokyo: 923–8. doi:10.1093/oxfordjournals.jbchem.a132624. PMID 500588.
- Lobelle-Rich PA, Reeves RE (1983). "Separation and characterization of two UTP-utilizing hexose phosphate uridylyltransferases from Entamoeba histolytica". Mol. Biochem. Parasitol. 7 (2): 173–82. doi:10.1016/0166-6851(83)90043-9. PMID 6304512.
Transferases: phosphorus-containing groups (EC 2.7) | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
2.7.1-2.7.4: phosphotransferase/kinase (PO4) |
| ||||||||||||||
2.7.6: diphosphotransferase (P2O7) | |||||||||||||||
2.7.7: nucleotidyltransferase (PO4-nucleoside) |
| ||||||||||||||
2.7.8: miscellaneous |
| ||||||||||||||
2.7.10-2.7.13: protein kinase (PO4; protein acceptor) |
|
Enzymes | |
---|---|
Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
|
This EC 2.7 enzyme-related article is a stub. You can help Misplaced Pages by expanding it. |