GMP synthase (glutamine—hydrolysing)

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GMP synthetase
PDB 1gpm EBI.jpg
Crystal structure of GMP synthetase.[1]
EC number
CAS number 37318-71-1
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO
GMP synthetase C terminal domain
PDB 1gpm EBI.jpg
escherichia coli gmp synthetase complexed with amp and pyrophosphate
Symbol GMP_synt_C
Pfam PF00958
InterPro IPR001674
SCOP 1gpm
Guanine monphosphate synthase
Protein GMPS PDB 2VPI.png
Rendering based on PDB 2VPI.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbol GMPS
External IDs OMIM600358 MGI2448526 HomoloGene68367 ChEMBL: 5721 GeneCards: GMPS Gene
EC number
RNA expression pattern
PBB GE GMPS 214431 at tn.png
More reference expression data
Species Human Mouse
Entrez 8833 229363
Ensembl ENSG00000163655 ENSMUSG00000027823
UniProt P49915 Q3THK7
RefSeq (mRNA) NM_003875 NM_001033300
RefSeq (protein) NP_003866 NP_001028472
Location (UCSC) Chr 3:
155.59 – 155.66 Mb
Chr 3:
63.98 – 64.02 Mb
PubMed search [1] [2]

Guanosine monophosphate synthetase, (EC also known as GMPS is an enzyme that converts xanthosine monophosphate to guanosine monophosphate.[2]

In the de novo synthesis of purine nucleotides, IMP is the branch point metabolite at which point the pathway diverges to the synthesis of either guanine or adenine nucleotides. In the guanine nucleotide pathway, there are 2 enzymes involved in converting IMP to GMP, namely IMP dehydrogenase (IMPD1), which catalyzes the oxidation of IMP to XMP, and GMP synthetase, which catalyzes the amination of XMP to GMP.[2]


In enzymology, a GMP synthetase (glutamine-hydrolysing) (EC is an enzyme that catalyzes the chemical reaction

ATP + xanthosine 5'-phosphate + L-glutamine + H2O \rightleftharpoons 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[edit]

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1GPM, 1WL8, 2A9V, 2D7J, and 2DPL.


  1. ^ Tesmer JJ, Klem TJ, Deras ML, Davisson VJ, Smith JL (January 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. 
  2. ^ a b "Entrez Gene: GMPS guanine monphosphate synthetase". 

Further reading[edit]

External links[edit]