Glucose-1-phosphate adenylyltransferase
| Glucose-1-phosphate adenylyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Glucose-1-phosphate adenylyltransferase tetramer, Rhizobium radiobacter | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.7.27 | ||||||||
| CAS no. | 9027-71-8 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from Arthrobacter and spinach combines adenosine triphosphate and glucose 1-phosphate to give adenosine diphosphate glucose (ADP-glucose), with pyrophosphate (PPi) as a byproduct.[1][2]
The reaction is part of starch, sucrose, and glycogen metabolism in bacteria. The rate limiting step in their synthesis is regulated at the level of this enzyme. In many species glycolytic intermediates act to stimulate enzyme activity while adenosine monophosphate or phosphate inhibit enzyme activity. In contrast, in many animals, the synthesis of alpha 1,4 glucans (glycogen) uses UDP-glucose as a glucose donor. In this case, the regulated step is instead the glycosyl transferase.[3][4]
Nomenclature
This enzyme is a transferase, specifically one 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.[5]
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1YP2, PDB: 1YP3, and PDB: 1YP4.
References
- ↑ 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 (6): 2334–2340. doi:10.1016/S0021-9258(18)97327-8. PMID 14304834.
- ↑ 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. doi:10.1016/S0021-9258(18)99747-4. PMID 5922972.
- ↑ Lee, Kenric; Doello, Sofia; Hagemann, Martin; Forchhammer, Karl (2025). "Deciphering the tight metabolite-level regulation of glucose-1-phosphate adenylyltransferase ( GLGC ) for glycogen synthesis in cyanobacteria". The FEBS Journal. 292 (4): 759–775. doi:10.1111/febs.17348. PMC 11839907. PMID 39639537.
- ↑ Ballicora, Miguel A.; Iglesias, Alberto A.; Preiss, Jack (2003). "ADP-Glucose Pyrophosphorylase, a Regulatory Enzyme for Bacterial Glycogen Synthesis". Microbiology and Molecular Biology Reviews. 67 (2): 213–225. doi:10.1128/mmbr.67.2.213-225.2003. PMC 156471. PMID 12794190.
- ↑ Enzyme 2.7.7.27 at KEGG Pathway Database.