Mannose-1-phosphate guanylyltransferase
| 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 | ||||||||
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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
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
[edit]As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2CU2.
References
[edit]- 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 (10): 3119–26. doi:10.1016/S0021-9258(18)97692-1. PMID 14245350.
