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Information on EC 6.3.5.2 - GMP synthase (glutamine-hydrolysing) and Organism(s) Homo sapiens and UniProt Accession P49915
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6.3.5.2 GMP synthase (glutamine-hydrolysing)IUBMB Comments
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.
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Word Map
- 6.3.5.2
- purine
- glutaminase
- anthranilate
- imp
- decoyinine
- acivicin
-
glutamine-dependent
-
ammonia-dependent
- gatcab
- tiazofurin
- 6-diazo-5-oxo-l-norleucine
- amidophosphoribosyltransferase
-
nh3-dependent
- synthesis
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
glutamine amidotransferase, gmp synthetase, gmp synthase, gatase, guanosine monophosphate synthetase, guanosine 5'-monophosphate synthetase, guanine monophosphate synthetase, xmp aminase, pd0279, gmp synthase (glutamine-hydrolysing), 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Glutamine amidotransferase
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-
-
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GMP synthase
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-
-
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GMP synthetase
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-
-
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GMP synthetase (glutamine hydrolysing)
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-
-
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GMPS
Guanosine 5'-monophosphate synthetase
Guanosine 5-monophosphate synthetase
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-
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Guanosine monophosphate synthetase (glutamine-hydrolyzing)
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-
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Guanylate synthetase
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-
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Guanylate synthetase (glutamine-hydrolyzing)
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-
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Synthetase, guanylate
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Xanthosine 5'-phosphate amidotransferase
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-
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Xanthosine 5-monophosphate aminase
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-
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Xanthosine-5'-phosphate-ammonia ligase
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-
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Xanthosine-5'-phosphate:ammonia ligase (AMP-forming)
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-
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Xanthosine-5'-phosphate:L-glutamine amido-ligase (AMP-forming)
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-
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XMP aminase
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-
-
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GMPS
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Guanosine 5'-monophosphate synthetase
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-
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amination
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-
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-
PATHWAY SOURCE
PATHWAYS
BRENDA
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-
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY
37318-71-1
not distinguished from EC 6.3.4.1
9023-55-6
EC 6.3.4.1
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + XMP + L-glutamine + H2O
AMP + diphosphate + GMP + L-glutamate
the N-terminal glutaminase domain of the enzyme generates ammonia from glutamine and the C-terminal synthetase domain aminates xanthine monophosphate to form GMP
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-
?
additional information
?
-
-
key enzyme in the de novo synthesis of guanine nucleotides
-
-
?
additional information
?
-
-
key enzyme in the de novo synthesis of guanine nucleotides
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-
?
additional information
?
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-
the enzyme is essential for de novo purine synthesis. Translocations of the MLL gene at chromosome band 11q23 are prevalent in patients with leukemia after treatment with epipodiphyllotoxins and other DNA topoisomerase II inhibitors. The MLL gene fuses with one of many different partner genes. GMPS is the first partner gene of MLL on chromosome 3Q and the first gene of this type in leukemia-associated translocations
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + XMP + L-glutamine + H2O
AMP + diphosphate + GMP + L-glutamate
the N-terminal glutaminase domain of the enzyme generates ammonia from glutamine and the C-terminal synthetase domain aminates xanthine monophosphate to form GMP
-
-
?
additional information
?
-
-
key enzyme in the de novo synthesis of guanine nucleotides
-
-
?
additional information
?
-
-
key enzyme in the de novo synthesis of guanine nucleotides
-
-
?
additional information
?
-
-
the enzyme is essential for de novo purine synthesis. Translocations of the MLL gene at chromosome band 11q23 are prevalent in patients with leukemia after treatment with epipodiphyllotoxins and other DNA topoisomerase II inhibitors. The MLL gene fuses with one of many different partner genes. GMPS is the first partner gene of MLL on chromosome 3Q and the first gene of this type in leukemia-associated translocations
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acivicin
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selectively abolishes glutaminase activity and Gln-dependent synthetase activity. No effect on NH4+-dependent synthetase activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GUAA_HUMAN
693
0
76715
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
77360
-
1 * 77360, density gradient centrifugation and subsequent electrospray MS analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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1 * 77360, density gradient centrifugation and subsequent electrospray MS analysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with XMP, sitting drop vapor diffusion method, using 0.1 M sodium acetate trihydrate, pH 5.2, 1.6 M ammonium sulfate, and 0.2 M sodium chloride, at 25°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-charged HiTrap chelating column chromatography and Superdex 200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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importance of guanine synthesis in immune cell function, GMP synthetase is a potential target for immunosuppressive therapy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hirst, M.; Haliday, E.; Nakamura, J.; Lou, L.
Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA
J. Biol. Chem.
269
23830-23837
1994
Homo sapiens
Nakamura, J.; Lou, L.
Biochemical characterization of human GMP synthetase
J. Biol. Chem.
270
7347-7353
1995
Homo sapiens
Nakamura, J.; Straub, K.; Wu, J.; Lou, L.
The glutamine hydrolysis function of human GMP synthetase. Identification of an essential active site cysteine
J. Biol. Chem.
270
23450-23455
1995
Homo sapiens
Lou, L.; Nakamura, J.; Tsing, S.; Nguyen, B.; Chow, J.; Straub, K.; Chan, H.; Barnett, J.
High-level production from a baculovirus expression system and biochemical characterization of human GMP synthetase
Protein Expr. Purif.
6
487-495
1995
Homo sapiens
Pegram, L.D.; Megonigal, M.D.; Lange, B.J.; Nowell, P.C.; Rowley, J.D.; Rappaport, E.F.; Felix, C.A.
t(1;11) translocation in treatment-related acute myeloid leukemia fuses MLL with the GMPS (guanosine 5' monophosphate synthetase) gene
Blood
96
4360-4362
2000
Homo sapiens
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