Nucleoside-triphosphate-aldose-1-phosphate nucleotidyltransferase
In enzymology, a nucleoside-triphosphate-aldose-1-phosphate nucleotidyltransferase (EC 2.7.7.28) is an enzyme that catalyzes the chemical reaction
- nucleoside triphosphate + alpha-D-aldose 1-phosphate diphosphate + NDP-hexose
| nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.28 | ||||||||
| CAS no. | 37278-26-5 | ||||||||
| 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 | ||||||||
| |||||||||
Thus, the two substrates of this enzyme are nucleoside triphosphate and alpha-D-aldose 1-phosphate, whereas its two products are diphosphate and NDP-hexose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is NTP:alpha-D-aldose-1-phosphate nucleotidyltransferase. Other names in common use include NDP hexose pyrophosphorylase, hexose 1-phosphate nucleotidyltransferase, hexose nucleotidylating enzyme, nucleoside diphosphohexose pyrophosphorylase, hexose-1-phosphate guanylyltransferase, GTP:alpha-D-hexose-1-phosphate guanylyltransferase, GDP hexose pyrophosphorylase, guanosine diphosphohexose pyrophosphorylase, nucleoside-triphosphate-hexose-1-phosphate nucleotidyltransferase, and NTP:hexose-1-phosphate nucleotidyltransferase.
References
- Verachtert H, Rodriguez P, Bass ST, Hansen RG (1966). "Purification and properties of guanosine diphosphate hexose pyrophosphorylase from mammalian tissues". J. Biol. Chem. 241 (9): 2007–13. PMID 5946626.
- Hansen RG, Verachtert H, Rodriguez P, Bass ST (1966). "GDP-hexose pyrophosphorylase from liver". Methods Enzymol. Methods in Enzymology. 8: 269–271. doi:10.1016/0076-6879(66)08048-0. ISBN 978-0-12-181808-1.