Mannose-1-phosphate guanylyltransferase
In enzymology, a mannose-1-phosphate guanylyltransferase (EC 2.7.7.13) is an enzyme that catalyzes the chemical reaction
- GTP + alpha-D-mannose 1-phosphate diphosphate + GDP-mannose
| mannose-1-phosphate guanylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.7.13 | ||||||||
| CAS no. | 37278-24-3 | ||||||||
| 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 GTP and alpha-D-mannose 1-phosphate, whereas its two products are diphosphate and GDP-mannose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is GTP:alpha-D-mannose-1-phosphate guanylyltransferase. Other names in common use include GTP-mannose-1-phosphate guanylyltransferase, PIM-GMP (phosphomannose isomerase-guanosine 5'-diphospho-D-mannose, pyrophosphorylase), GDP-mannose pyrophosphorylase, guanosine 5'-diphospho-D-mannose pyrophosphorylase, guanosine diphosphomannose pyrophosphorylase, guanosine triphosphate-mannose 1-phosphate guanylyltransferase, and mannose 1-phosphate guanylyltransferase (guanosine triphosphate). This enzyme participates in fructose and mannose metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2CU2.
References
- Munch-Peterson A (1955). "Enzymatic synthesis and phosphorolysis of guanosine diphosphate mannose". Arch. Biochem. Biophys. 55 (2): 592–593. doi:10.1016/0003-9861(55)90441-0.
- PREISS J, WOOD E (1964). "Sugar Nucleotide Reactions in Arthrobacter. I. Guanosine Diphosphate Mannose Pyrophosphorylase: Purification and Properties". J. Biol. Chem. 239: 3119–26. PMID 14245350.