Biology:GMP synthase (glutamine—hydrolysing)
| GMP synthetase (glutamine-hydrolyzing) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 GMP synthetase, human | |||||||||
| Identifiers | |||||||||
| EC number | 6.3.5.2 | ||||||||
| CAS number | 37318-71-1 | ||||||||
| 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 | ||||||||
| |||||||||
| GMP synthetase C terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 escherichia coli gmp synthetase complexed with amp and pyrophosphate.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | GMP_synt_C | ||||||||
| Pfam | PF00958 | ||||||||
| InterPro | IPR001674 | ||||||||
| PROSITE | PDOC00405 | ||||||||
| SCOP2 | 1gpm / SCOPe / SUPFAM | ||||||||
| |||||||||
 Generic protein structure example |
Guanosine monophosphate synthetase, (EC 6.3.5.2) also known as GMPS is an enzyme that converts xanthosine monophosphate to guanosine monophosphate.[2]
Enzymology
In enzymology, a GMP synthetase (glutamine-hydrolysing) (EC 6.3.5.2) is an enzyme that catalyzes the chemical reaction
- ATP + xanthosine 5'-phosphate + L-glutamine + H2O [math]\displaystyle{ \rightleftharpoons }[/math] AMP + diphosphate + GMP + L-glutamate
The 4 substrates of this enzyme are ATP, xanthosine 5'-phosphate, L-glutamine, and H2O, whereas its 4 products are AMP, diphosphate, GMP, and L-glutamate.
This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds carbon-nitrogen ligases with glutamine as amido-N-donor. The systematic name of this enzyme class is xanthosine-5'-phosphate:L-glutamine amido-ligase (AMP-forming). Other names in common use include GMP synthetase (glutamine-hydrolysing), guanylate synthetase (glutamine-hydrolyzing), guanosine monophosphate synthetase (glutamine-hydrolyzing), xanthosine 5'-phosphate amidotransferase, and guanosine 5'-monophosphate synthetase. This enzyme participates in purine metabolism and glutamate metabolism. At least one compound, Psicofuranin is known to inhibit this enzyme.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1GPM, 1WL8, 2A9V, 2D7J, and 2DPL.
References
- ↑ "The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families". Nat. Struct. Biol. 3 (1): 74–86. January 1996. doi:10.1038/nsb0196-74. PMID 8548458.
- ↑ "Entrez Gene: GMPS guanine monphosphate synthetase". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8833.
Further reading
- "Biosynthesis of nucleic acid purines. III. Guanosine 5'-phosphate formation from xanthosine 5'-phosphate and L-glutamine". Arch. Biochem. Biophys. 79: 91–110. 1959. doi:10.1016/0003-9861(59)90383-2.
- LAGERKVIST U (1958). "Biosynthesis of guanosine 5'-phosphate. II. Amination of xanthosine 5'-phosphate by purified enzyme from pigeon liver". J. Biol. Chem. 233 (1): 143–9. PMID 13563458.
External links
- GMP+synthetase at the US National Library of Medicine Medical Subject Headings (MeSH)
 |
