EC - GMP synthase (glutamine-hydrolysing)

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IntEnz Enzyme Nomenclature


Accepted name:
GMP synthase (glutamine-hydrolysing)
Other names:
GMP synthetase (glutamine-hydrolysing)
guanosine 5'-monophosphate synthetase
guanosine monophosphate synthetase (glutamine-hydrolyzing)
guanylate synthetase (glutamine-hydrolyzing)
xanthosine 5'-phosphate amidotransferase
Systematic name:
xanthosine-5'-phosphate:L-glutamine amido-ligase (AMP-forming)



Involved in the de novo biosynthesis of guanosine nucleotides. An N-terminal glutaminase domain binds L-glutamine and generates ammonia, which is transferred by a substrate-protective tunnel to the ATP-pyrophosphatase domain. The enzyme can catalyse the second reaction alone in the presence of ammonia. Formerly EC

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00405
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003922
CAS Registry Number: 37318-71-1
UniProtKB/Swiss-Prot: (663) [show] [UniProt]


  1. Lagerkvist, U.
    Biosynthesis of guanosine 5'-phosphate. II. Amination of xanthosine 5'-phosphate by purified enzyme from pigeon liver.
    J. Biol. Chem. 233 : 143-149 (1958). [PMID: 13563458]
  2. Abrams, R. and Bentley, M.
    Biosynthesis of nucleic acid purines. III. Guanosine 5'-phosphate formation from xanthosine 5'-phosphate and L-glutamine.
    Arch. Biochem. Biophys. 79 : 91-110 (1959).
  3. Zalkin, H., Argos, P., Narayana, S. V., Tiedeman, A. A., Smith, J. M.
    Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase.
    J. Biol. Chem. 260 : 3350-3354 (1985). [PMID: 2982857]
  4. Abbott, J. L., Newell, J. M., Lightcap, C. M., Olanich, M. E., Loughlin, D. T., Weller, M. A., Lam, G., Pollack, S., Patton, W. A.
    The effects of removing the GAT domain from E. coli GMP synthetase.
    Protein J. 25 : 483-491 (2006). [PMID: 17103135]

[EC created 1961, modified 2013]