6.3.5.2: GMP synthase (glutamine-hydrolysing)
This is an abbreviated version!
For detailed information about GMP synthase (glutamine-hydrolysing), go to the full flat file.
Word Map on EC 6.3.5.2
-
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
- 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
Reaction
Synonyms
cgsA, di-GMP synthase A, EC 6.3.4.1, GATase, Glutamine amidotransferase, GMP synthase, GMP synthase [glutamine-hydrolyzing] subunit B, GMP synthetase, GMP synthetase (glutamine hydrolysing), GMPS, GUA, GuaA, Guanine monophosphate synthetase, Guanosine 5'-monophosphate synthetase, Guanosine 5-monophosphate synthetase, guanosine monophosphate synthetase, Guanosine monophosphate synthetase (glutamine-hydrolyzing), Guanylate synthetase, Guanylate synthetase (glutamine-hydrolyzing), More, PD0279, PH1346, Synthetase, guanylate, two-subunit-type GMP synthetase, Xanthosine 5'-phosphate amidotransferase, Xanthosine 5-monophosphate aminase, Xanthosine-5'-phosphate-ammonia ligase, Xanthosine-5'-phosphate:ammonia ligase (AMP-forming), Xanthosine-5'-phosphate:L-glutamine amido-ligase (AMP-forming), XMP aminase
ECTree
6.3.5.2 GMP synthase (glutamine-hydrolysing)Advanced search results
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results (Substrates Products
Substrates Products on EC 6.3.5.2 - GMP synthase (glutamine-hydrolysing)
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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 + 1-ribosyl-4,6-dihydroxypyrazolo[3,4-d]-pyrimidine 5-phosphate
AMP + phosphate + 1-ribosyl-4-hydroxy-6-aminopyrazolo[3,4-d]pyrimidine 5'-phosphate
ATP + beta-arabinofuranosyl-XMP
AMP + phosphate + beta-arabinofuranosylGMP
-
-
-
-
?
ATP + 1-ribosyl-4,6-dihydroxypyrazolo[3,4-d]-pyrimidine 5-phosphate
AMP + phosphate + 1-ribosyl-4-hydroxy-6-aminopyrazolo[3,4-d]pyrimidine 5'-phosphate
-
-
-
?
ATP + 1-ribosyl-4,6-dihydroxypyrazolo[3,4-d]-pyrimidine 5-phosphate
AMP + phosphate + 1-ribosyl-4-hydroxy-6-aminopyrazolo[3,4-d]pyrimidine 5'-phosphate
-
-
-
?
ATP + 1-ribosyl-4,6-dihydroxypyrazolo[3,4-d]-pyrimidine 5-phosphate
AMP + phosphate + 1-ribosyl-4-hydroxy-6-aminopyrazolo[3,4-d]pyrimidine 5'-phosphate
-
-
-
-
?
ATP + dXMP + NH4+
AMP + phosphate + dGMP
-
at 4.3% of the activity relative to XMP
-
-
?
ATP + xanthosine 5'-phosphate + Gln
AMP + diphosphate + Glu
-
-
-
-
?
ATP + xanthosine 5'-phosphate + L-glutamine + H2O
AMP + diphosphate + GMP + L-glutamate
-
-
-
?
ATP + xanthosine 5'-phosphate + L-glutamine + H2O
AMP + diphosphate + GMP + L-glutamate
-
-
?
ATP + xanthosine 5'-phosphate + L-glutamine + H2O
AMP + diphosphate + GMP + L-glutamate
GMP synthetase catalyzes the conversion of XMP to GMP. Ammonia, generated in the amino-terminal glutamine amidotransferase (GAT) domain, is transferred to the ATP-pyrophosphatase (ATPP) domain, where it attacks a highly reactive adenyl-XMP intermediate, leading to GMP formation
-
-
?
ATP + xanthosine 5'-phosphate + L-glutamine + H2O
AMP + diphosphate + GMP + L-glutamate
-
steady state ordered binding of the substrates ATP and XMP to the ATPase domain, with ATP being the first substrate to bind followed by XMP
-
-
?
ATP + xanthosine 5'-phosphate + NH3
AMP + diphosphate + GMP
ATPP/DD (a construct that contains the ATP-pyrophosphatase domain as well as the predicted dimerization domain) expressed as both a His-tagged fusion protein (His-ATPP/DD) and as a non-fusion protein (NF-ATPP/DD) is capable of catalyzing the conversion of XMP to GMP using exogenously added ammonia
-
-
?
ATP + xanthosine 5'-phosphate + NH3
AMP + diphosphate + GMP
overall reaction
-
-
?
ATP + xanthosine 5'-phosphate + NH3
AMP + diphosphate + GMP
overall reaction
-
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
identical Km value for NH4+ and Gln
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
identical Km value for NH4+ and Gln
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
it was previously reported that the activity responsible for GMP synthesis is strictly NH4+-dependent. It is possible that the glutamine-dependent activity is inactivated by Tris in the previously used 30-min end point assay
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
Gln-dependent activity is approximately 2times more active than the NH4+-dependent activity
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
maximal rate of the Gln-dependent activity is about 35% greater than that of NH4+-dependent activity
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
a single enzyme is responsible for Gln-dependent and NH4+ dependent reaction
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
Escherichia coli B / ATCC 11303
-
a single enzyme is responsible for Gln-dependent and NH4+ dependent reaction
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
identical Km value for NH4+ and Gln
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
a single enzyme is responsible for Gln-dependent and NH4+ dependent reaction
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
identical Km value for NH4+ and Gln
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
Gln-dependent activity is approximately 2times more active than the NH4+-dependent activity
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
higher Km value for NH4+ compared with Gln
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
higher Km value for NH4+ compared with Gln
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
Pigeon
-
maximal rate of NH4+-dependent activity is 15% of that obtained with L-Gln
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
maximal activity with NH4+ is 80% of that obtained with Gln
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
higher Km value for NH4+ compared with Gln
-
?
ATP + XMP + L-Gln
AMP + diphosphate + GMP + L-Glu
-
enzyme can use both glutamine and external ammonia, the kinetic parameters kcat and Km for the two substrates are different and also exhibit a pH-dependent change
-
-
?
ATP + XMP + L-glutamine + H2O
AMP + diphosphate + GMP + L-glutamate
-
-
-
-
?
ATP + XMP + L-glutamine + H2O
AMP + diphosphate + GMP + L-glutamate
-
-
-
?
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
-
-
?
ATP + XMP + L-glutamine + H2O
AMP + diphosphate + GMP + L-glutamate
-
-
-
-
?
ATP + XMP + L-glutamine + H2O
AMP + diphosphate + GMP + L-glutamate
-
-
-
-
?
ATP + XMP + L-glutamine + H2O
AMP + diphosphate + GMP + L-glutamate
-
-
-
-
?
ATP + XMP + NH3
AMP + diphosphate + GMP
-
enzyme can use both glutamine and external ammonia, the kinetic parameters kcat and Km for the two substrates are different and also exhibit a pH-dependent change
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
substrates not mentioned:
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
identical Km value for NH4+ and Gln
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
identical Km value for NH4+ and Gln
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
it was previously reported that the activity responsible for GMP synthesis is strictly NH4+-dependent. It is possible that the glutamine-dependent activity is inactivated by Tris in the previously used 30-min end point assay
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
Gln-dependent activity is approximately 2times more active than the NH4+-dependent activity
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
maximal rate of the Gln-dependent activity is about 35% greater than that of NH4+-dependent activity
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
a single enzyme is responsible for Gln-dependent and NH4+ dependent reaction
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
Escherichia coli B / ATCC 11303
-
a single enzyme is responsible for Gln-dependent and NH4+ dependent reaction
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
it was previously reported that the activity responsible for GMP synthesis is strictly NH4+-dependent. It is possible that the glutamine-dependent activity is inactivated by Tris in the previously used 30-min end point assay
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
maximal rate of the Gln-dependent activity is about 35% greater than that of NH4+-dependent activity
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
identical Km value for NH4+ and Gln
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
a single enzyme is responsible for Gln-dependent and NH4+ dependent reaction
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
identical Km value for NH4+ and Gln
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
Gln-dependent activity is approximately 2times more active than the NH4+-dependent activity
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
higher Km value for NH4+ compared with Gln
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
higher Km value for NH4+ compared with Gln
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
Pigeon
-
maximal rate of NH4+-dependent activity is 15% of that obtained with L-Gln
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
NH4+ in form of (NH4)2SO4
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
maximal activity with NH4+ is 80% of that obtained with Gln
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
higher Km value for NH4+ compared with Gln
-
?
L-glutamine + H2O
L-glutamate + NH3
GATase half-reaction, structure-activity relationship of the functional subunits, overview
-
-
?
L-glutamine + H2O
L-glutamate + NH3
GATase half-reaction, structure-activity relationship of the functional subunits, overview
-
-
?
XMP + Mg-ATP2-
adenyl-XMP + diphosphate + Mg2+
ATPPase half-reaction, structure-activity relationship of the functional subunits, overview
adenyl-XMP is the overall reaction intermediate
-
?
XMP + Mg-ATP2-
adenyl-XMP + diphosphate + Mg2+
ATPPase half-reaction, structure-activity relationship of the functional subunits, overview
adenyl-XMP is the overall reaction intermediate
-
?
additional information
?
-
-
GMP synthetase binds ubiquitin-specific protease 7, USP7, and deubiquitylates histone H2B, the GMPS/USP7 complex cooperates with the Polycomb silencing system through removal of the active ubiquitin mark from histone H2B. GMPS/USP7 binds ecdysone-regulated loci prior to or after hormone signaling. The Ecdysone receptor interacts biochemically and genetically with GMPS/USP7
-
-
?
additional information
?
-
Drosophila sp. (in: flies)
-
GMP synthetase stimulates histone H2B deubiquitylation by the epigenetic silencer USP7, GMP synthetase can regulate chromatin silencing via modulation of H2B deubiquitylation by USP7
-
-
?
additional information
?
-
-
maximal rate of glutaminase activity is 1.8fold greater than GMP synthetase activity
-
-
?
additional information
?
-
-
it was previously reported that the activity responsible for GMP synthesis is strictly NH4+-dependent. It is possible that the Gln-dependent activity is inactivated by Tris in the previously used 30-min end point assay
-
-
?
additional information
?
-
-
final step of de novo guanine nucleotide biosynthesis
-
-
?
additional information
?
-
-
maximal rate of glutaminase activity is 1.8fold greater than GMP synthetase activity
-
-
?
additional information
?
-
-
it was previously reported that the activity responsible for GMP synthesis is strictly NH4+-dependent. It is possible that the Gln-dependent activity is inactivated by Tris in the previously used 30-min end point assay
-
-
?
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
-
-
?
additional information
?
-
-
no substrates mentioned
-
-
?
additional information
?
-
-
enzyme of the purine salvage pathway
-
-
?
additional information
?
-
-
no substrates mentioned
-
-
?
additional information
?
-
-
enzyme of the purine salvage pathway
-
-
?
additional information
?
-
GMP is necessary for DNA and RNA synthesis. Expression of the gene encoding GMP synthase coincides with the points in the life cycle with increased DNA and RNA synthesis
-
-
?
additional information
?
-
-
GMP is necessary for DNA and RNA synthesis. Expression of the gene encoding GMP synthase coincides with the points in the life cycle with increased DNA and RNA synthesis
-
-
?
additional information
?
-
GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase, GATase, and ATP pyrophosphatase, ATPPase. GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATPPase utilizes ammonia to convert adenyl-XMP into guanosine 5'-monophosphate. The GATase subunit of the two-subunit-type GMPS alone is inactiv
-
-
?
additional information
?
-
GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase, GATase, and ATP pyrophosphatase, ATPPase. GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATPPase utilizes ammonia to convert adenyl-XMP into guanosine 5'-monophosphate. The GATase subunit of the two-subunit-type GMPS alone is inactiv
-
-
?
additional information
?
-
-
GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase, GATase, and ATP pyrophosphatase, ATPPase. GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATPPase utilizes ammonia to convert adenyl-XMP into guanosine 5'-monophosphate. The GATase subunit of the two-subunit-type GMPS alone is inactiv
-
-
?
additional information
?
-
GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase, GATase, and ATP pyrophosphatase, ATPPase. GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATPPase utilizes ammonia to convert adenyl-XMP into guanosine 5'-monophosphate. The GATase subunit of the two-subunit-type GMPS alone is inactiv
-
-
?
additional information
?
-
GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase, GATase, and ATP pyrophosphatase, ATPPase. GATase hydrolyzes glutamine to yield glutamate and ammonia, while ATPPase utilizes ammonia to convert adenyl-XMP into guanosine 5'-monophosphate. The GATase subunit of the two-subunit-type GMPS alone is inactiv
-
-
?
additional information
?
-
-
enzyme activity is linked with cellular proliferation in differentiating, regenerating and neoplastic tissues
-
-
?
additional information
?
-
-
enzyme of the purine salvage pathway
-
-
?
additional information
?
-
-
enzyme of the purine salvage pathway
-
-
?
