GMP synthase: Difference between revisions
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*{{cite journal | author=Page T, Bakay B, Nyhan WL |title=Human GMP synthetase. |journal=Int. J. Biochem. |volume=16 |issue= 1 |pages= 117–20 |year= 1984 |pmid= 6698284 |doi=10.1016/0020-711X(84)90061-2 }} |
*{{cite journal | author=Page T, Bakay B, Nyhan WL |title=Human GMP synthetase. |journal=Int. J. Biochem. |volume=16 |issue= 1 |pages= 117–20 |year= 1984 |pmid= 6698284 |doi=10.1016/0020-711X(84)90061-2 }} |
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*{{cite journal | author=Nakamura J, Straub K, Wu J, Lou L |title=The glutamine hydrolysis function of human GMP synthetase. Identification of an essential active site cysteine. |journal=J. Biol. Chem. |volume=270 |issue= 40 |pages= 23450–5 |year= 1995 |pmid= 7559506 |doi= |
*{{cite journal | author=Nakamura J, Straub K, Wu J, Lou L |title=The glutamine hydrolysis function of human GMP synthetase. Identification of an essential active site cysteine. |journal=J. Biol. Chem. |volume=270 |issue= 40 |pages= 23450–5 |year= 1995 |pmid= 7559506 |doi= }} |
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*{{cite journal | author=Nakamura J, Lou L |title=Biochemical characterization of human GMP synthetase. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7347–53 |year= 1995 |pmid= 7706277 |doi= |
*{{cite journal | author=Nakamura J, Lou L |title=Biochemical characterization of human GMP synthetase. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7347–53 |year= 1995 |pmid= 7706277 |doi= }} |
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*{{cite journal | author=Hirst M, Haliday E, Nakamura J, Lou L |title=Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA. |journal=J. Biol. Chem. |volume=269 |issue= 38 |pages= 23830–7 |year= 1994 |pmid= 8089153 |doi= }} |
*{{cite journal | author=Hirst M, Haliday E, Nakamura J, Lou L |title=Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA. |journal=J. Biol. Chem. |volume=269 |issue= 38 |pages= 23830–7 |year= 1994 |pmid= 8089153 |doi= }} |
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*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }} |
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }} |
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Revision as of 14:22, 10 February 2011
| GMP synthase (glutamine-hydrolyzing) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Crystal structure of GMP synthase.[1] | |||||||||
| Identifiers | |||||||||
| EC no. | 6.3.5.2 | ||||||||
| CAS no. | 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 | ||||||||
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Template:FixBunching Template:PBB Template:FixBunching Guanine monphosphate 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 synthase (glutamine-hydrolysing) (EC 6.3.5.2) is an enzyme that catalyzes the chemical reaction
- ATP + xanthosine 5'-phosphate + L-glutamine + H2O 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
- ^ Tesmer JJ, Klem TJ, Deras ML, Davisson VJ, Smith JL (1996). "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. doi:10.1038/nsb0196-74. PMID 8548458.
{{cite journal}}: Unknown parameter|month=ignored (help)CS1 maint: multiple names: authors list (link) - ^ "Entrez Gene: GMPS guanine monphosphate synthetase".
Further reading
- Abrams R and Bentley M (1959). "Biosynthesis of nucleic acid purines. III. Guanosine 5'-phosphate formation from xanthosine 5'-phosphate and L-glutamine". Arch. Biochem. Biophys. 79: 91–110. 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+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)