Glucose-1-phosphate adenylyltransferase

In enzymology, a glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) is an enzyme that catalyzes the chemical reaction

ATP + alpha-D-glucose 1-phosphate diphosphate + ADP-glucose
glucose-1-phosphate adenylyltransferase
Glucose-1-phosphate adenylyltransferase tetramer, Rhizobium radiobacter
Identifiers
EC no.2.7.7.27
CAS no.9027-71-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Thus, the two substrates of this enzyme are ATP and alpha-D-glucose 1-phosphate, whereas its two products are diphosphate and ADP-glucose.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:alpha-D-glucose-1-phosphate adenylyltransferase. Other names in common use include ADP glucose pyrophosphorylase, glucose 1-phosphate adenylyltransferase, adenosine diphosphate glucose pyrophosphorylase, adenosine diphosphoglucose pyrophosphorylase, ADP-glucose pyrophosphorylase, ADP-glucose synthase, ADP-glucose synthetase, ADPG pyrophosphorylase, ADP:alpha-D-glucose-1-phosphate adenylyltransferase and AGPase. This enzyme participates in starch and sucrose metabolism.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1YP2, 1YP3, and 1YP4.

References

    • Ghosh HP, Preiss J (1966). "Adenosine diphosphate glucose pyrophosphorylase. A regulatory enzyme in the biosynthesis of starch in spinach leaf chloroplasts". J. Biol. Chem. 241 (19): 4491–504. PMID 5922972.
    • Shen L; Preiss J (1965). "Biosynthesis of bacterial glycogen. I. Purification and properties of the adenosine diphosphoglucose pyrophosphorylase of Arthrobacter species NRRL B1973". J. Biol. Chem. 240: 2334–2340. PMID 14304834.


    This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.