GMP synthase

GMP synthetase (glutamine-hydrolyzing)
Crystal structure of GMP synthetase.
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
Search PMC articles PubMed articles NCBI proteins

GMP synthetase C terminal domain
escherichia coli gmp synthetase complexed with amp and pyrophosphate
Identifiers
Symbol	GMP_synt_C
Pfam	PF00958
InterPro	IPR001674
PROSITE	PDOC00405
SCOP2	1gpm / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

GMPS
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2VPI, 2VXO
Identifiers
Aliases	GMPS, GMP synthase, guanine monophosphate synthase, GATD7, GMP synthase
External IDs	OMIM: 600358; MGI: 2448526; HomoloGene: 68367; GeneCards: GMPS; OMA:GMPS - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3q25.31 Start 155,870,650 bp End 155,944,020 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 E1 Start 63,883,527 bp End 63,930,000 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left testis right testis ventricular zone ganglionic eminence stromal cell of endometrium Achilles tendon islet of Langerhans smooth muscle tissue body of pancreas epithelium of colon Top expressed in otic vesicle hand seminiferous tubule mandibular prominence maxillary prominence primitive streak abdominal wall Rostral migratory stream mammillary body dorsomedial hypothalamic nucleus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding ligase activity pyrophosphatase activity ATP binding GMP synthase (glutamine-hydrolyzing) activity GMP synthase activity Cellular component cytoplasm cytosol Biological process purine nucleotide biosynthetic process glutamine metabolic process purine nucleobase biosynthetic process purine ribonucleoside monophosphate biosynthetic process GMP biosynthetic process Sources:Amigo / QuickGO
Orthologs 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: 155.87 – 155.94 Mb Chr 3: 63.88 – 63.93 Mb PubMed search
Wikidata
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Guanosine monophosphate synthetase, (EC 6.3.5.2) also known as GMPS is an enzyme that converts xanthosine monophosphate to guanosine monophosphate.

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 $\rightleftharpoons$ 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

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

Further reading

• Abrams R, 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. {{cite journal}}: Unknown parameter |last-author-amp= ignored (|name-list-style= suggested) (help)
• 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 U.S. National Library of Medicine Medical Subject Headings (MeSH)