Biology:Glucose-1-phosphate cytidylyltransferase

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glucose-1-phosphate cytidylyltransferase
Identifiers
EC number2.7.7.33
CAS number9027-10-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, a glucose-1-phosphate cytidylyltransferase (EC 2.7.7.33) is an enzyme that catalyzes the chemical reaction

CTP + alpha-D-glucose 1-phosphate [math]\displaystyle{ \rightleftharpoons }[/math] diphosphate + CDP-glucose

Thus, the two substrates of this enzyme are CTP and alpha-D-glucose 1-phosphate, whereas its two products are diphosphate and CDP-glucose.[1][2]

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:alpha-D-glucose-1-phosphate cytidylyltransferase. Other names in common use include CDP glucose pyrophosphorylase, cytidine diphosphoglucose pyrophosphorylase, cytidine diphosphate glucose pyrophosphorylase, cytidine diphosphate-D-glucose pyrophosphorylase, and CTP:D-glucose-1-phosphate cytidylyltransferase. This enzyme participates in starch and sucrose metabolism and nucleotide sugars metabolism.[3]

Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1TZF and 1WVC.

References

  1. "Biosynthesis of O-antigens: genes and pathways involved in nucleotide sugar precursor synthesis and O-antigen assembly". Carbohydr. Res. 338 (23): 2503–19. 2003. doi:10.1016/j.carres.2003.07.009. PMID 14670712. 
  2. Xue M. He; Hung-wen Liu (2002). "Formation of unusual sugars: Mechanistic studies and biosynthetic applications". Annu Rev Biochem 71: 701–754. doi:10.1146/annurev.biochem.71.110601.135339. PMID 12045109. 
  3. "Purification and Properties of Cytidine Diphosphate D-Glucose Pyrophosphorylase from Salmonella Paratyphi A". J. Biol. Chem. 240: 1900–4. 1965. PMID 14299608.