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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 + 6-thioXMP + NH4+
AMP + phosphate + 6-thioGMP
ATP + 8-azaXMP + NH4+
AMP + phosphate + 8-azaGMP
ATP + beta-arabinofuranosyl-XMP
AMP + phosphate + beta-arabinofuranosylGMP
-
-
-
-
?
ATP + dXMP + NH4+
AMP + phosphate + dGMP
ATP + xanthosine 5'-phosphate + Gln
AMP + diphosphate + Glu
ATP + xanthosine 5'-phosphate + L-glutamine + H2O
AMP + diphosphate + GMP + L-glutamate
ATP + xanthosine 5'-phosphate + NH3
AMP + diphosphate + GMP
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
ATP + XMP + L-Gln
AMP + diphosphate + GMP + L-Glu
ATP + XMP + L-glutamine + H2O
AMP + diphosphate + GMP + L-glutamate
ATP + XMP + NH3
AMP + diphosphate + GMP
ATP + XMP + NH4+
AMP + diphosphate + GMP
ATPgammaS + XMP + Gln
?
-
GMP formation is 10% that of ATP
-
-
?
L-glutamine + H2O
L-glutamate + NH3
XMP + Mg-ATP2-
adenyl-XMP + diphosphate + Mg2+
additional information
?
-
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 + 6-thioXMP + NH4+
AMP + phosphate + 6-thioGMP
-
-
-
?
ATP + 6-thioXMP + NH4+
AMP + phosphate + 6-thioGMP
-
-
-
?
ATP + 6-thioXMP + NH4+
AMP + phosphate + 6-thioGMP
-
-
-
-
?
ATP + 8-azaXMP + NH4+
AMP + phosphate + 8-azaGMP
-
-
-
?
ATP + 8-azaXMP + NH4+
AMP + phosphate + 8-azaGMP
-
-
-
?
ATP + 8-azaXMP + NH4+
AMP + phosphate + 8-azaGMP
-
-
-
-
?
ATP + dXMP + NH4+
AMP + phosphate + dGMP
-
-
-
-
?
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 + 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
-
-
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
-
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
-
-
?
ATP + XMP + Gln
AMP + diphosphate + GMP + Glu
-
-
-
?
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
-
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
-
-
-
?
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
-
-
-
?
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
-
ir
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
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
-
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
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
a single enzyme is responsible for Gln-dependent and NH4+ dependent reaction
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
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
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
ATP + XMP + NH4+
AMP + diphosphate + GMP
-
-
-
?
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
-
-
-
?
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
-
?
XMP + Mg-ATP2-
adenyl-XMP + diphosphate + Mg2+
-
-
-
-
?
additional information
?
-
-
no substrates mentioned
-
-
?
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
?
-
-
no substrates mentioned
-
-
?
additional information
?
-
-
no substrates mentioned
-
-
?
additional information
?
-
-
no substrates mentioned
-
-
?
additional information
?
-
-
glutaminase activity
-
-
?
additional information
?
-
-
glutaminase activity
-
-
?
additional information
?
-
-
glutaminase activity
-
-
?
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
?
-
-
glutaminase activity
-
-
?
additional information
?
-
-
glutaminase activity
-
-
?
additional information
?
-
-
no substrates mentioned
-
-
?
additional information
?
-
-
glutaminase activity
-
-
?
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
?
-
-
no substrates mentioned
-
-
?
additional information
?
-
-
no substrates mentioned
-
-
?
additional information
?
-
-
no substrates mentioned
-
-
?
additional information
?
-
-
no substrates mentioned
-
-
?
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
?
-
-
no substrates mentioned
-
-
?
additional information
?
-
-
no substrates mentioned
-
-
?
additional information
?
-
-
enzyme of the purine salvage pathway
-
-
?
additional information
?
-
-
enzyme of the purine salvage pathway
-
-
?
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(alpha-S,5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid
trivial name acivicin
1,N6-Ethenoadenosine 5'-triphosphate
-
-
1-Ribosyl-4,6-dihydroxypyrazolo[3,4-d]-pyrimidine 5'-phosphate
-
-
1-Ribosyl-4-hydroxy-6-aminopyrazolo[3,4-d]pyrimidine 5'-phosphate
-
-
2,6-diaminopurine ribonucleoside
-
-
2-Amino-6-methylthiopurine ribonucleoside
-
-
2-fluoroinosine 5'-monophosphate
-
50% inhibition above 2 mM
5'-Azido-5'-deoxyadenosine
-
-
5'-thioethyl-5'-deoxyadenosine
-
-
6-Amino-9-D-psicofuranosylpurine
6-Chloropurine ribonucleoside
-
-
6-diazo-5-oxo-L-norleucine
6-Methylmercaptopurine ribonucleoside
-
-
6-Methylpurine ribonucleoside
-
-
6-Methylpurine ribonucleotide
-
-
6-thioguanine
-
0.5 mM, 27% inhibition
8-Azaguanine
-
0.5 mM, 40% inhibition
adenine 9-beta-D-arabinofuranoside 5'-triphosphate
-
-
adenosine 5'-(beta,gamma-imido)triphosphate
-
non-competitive versus XMP, competitive versus ATP
AMP-PNP
-
potent inhibitor, competitive and non-competitive inhibitor with respect to ATP and XMP
beta,gamma-Imidoadenosine 5-triphosphate
-
-
Bredinin 5'-phosphate
-
-
GDP
-
0.5 mM, 42% inhibition
Glucofuranosyladenine
-
-
glutamic acid-gamma-methyl ester
-
competitive towards Gln
GTP
-
0.5 mM, 40% inhibition
guanidine hydrochloride
-
-
guanosine
-
0.5 mM, 50% inhibition
IMP
-
0.5 mM, 10% inhibition
iodoacetamide
-
inhibition of Gln-dependent activity, no inhibition of NH4+-dependent activity
kinetin ribonucleoside
-
-
L-2-Amino-4-oxo-5-chloropentanoic acid
-
inhibition of Gln-dependent activity and NH4+-dependent activity
N2-hydroxyguanosine 5'-monophosphate
-
0.0003-0.0005 mM, 50% inhibition
N6,N6-Dimethyladenosine
-
-
N6-Hydroxyaminopurine ribonucleoside
-
-
N6-isopentenyladenosine
-
-
Na+
-
25% loss of activity at 24 mM, 90% loss of activity at 200 mM
Nucleodide inhibitors
-
overview
-
XMP
-
substrate inhibition above 0.2 mM
zeatin ribonucleoside
-
-
additional information
-
not inhibitory at 0.5 mM: hypoxanthine, chloroadenosine, xanthosine, inosine, decoyinine
-
5'-deoxyadenosine
-
-
6-Amino-9-D-psicofuranosylpurine
-
strong inhibition of wild type enzyme, mutant enzyme GP-1 with decreased inhibition, complete loss of inhibition of mutant enzyme MG-1
6-Amino-9-D-psicofuranosylpurine
-
i.e. psicofuranine, irreversible inhibition, dependent on presence of XMP and diphosphate
6-Amino-9-D-psicofuranosylpurine
-
-
6-diazo-5-oxo-L-norleucine
-
-
6-diazo-5-oxo-L-norleucine
-
irreversible inhibition is dependent on presence of XMP, ATP and Mg2+
6-diazo-5-oxo-L-norleucine
-
irreversible inhibition of Gln-dependent activity
6-diazo-5-oxo-L-norleucine
-
inhibition of Gln-dependent activity and NH4+-dependent activity
6-diazo-5-oxo-L-norleucine
-
Gln-dependent activity is more sensitive than NH4+-dependent activity; inhibition of Gln-dependent activity and NH4+-dependent activity
6-diazo-5-oxo-L-norleucine
-
6-diazo-5-oxo-L-norleucine
-
irreversible inhibitor
6-thioXMP
-
-
acivicin
-
selectively abolishes glutaminase activity and Gln-dependent synthetase activity. No effect on NH4+-dependent synthetase activity
acivicin
-
irreversible inhibitor
adenosine
-
strong inhibition of wild type enzyme, mutant GP-1 with decreased inhibition, complete loss of inhibition in mutant MG-1
adenosine
-
0.5 mM, 37% inhibition
AMP
-
poor product inhibitor, competitive towards ATP
AMP
-
0.5 mM, 22% inhibitiion; 0.5 mM, 22% inhibition
ATP
-
substrate inhibition
Decoyinine
-
strong inhibition of wild type enzyme, and mutant enzyme GP-1, complete loss of inhibition in mutant MG-1
Decoyinine
-
uncompetitive towards Gln and XMP and noncompetitive towards ATP
diphosphate
-
competitive with respect to ATP; kinetic parameters for the two progressively formed inhibitory complexes
diphosphate
-
competitive with respect to ATP
diphosphate
-
non-competitive versus XMP, competitive versus ATP, non-competitive versus L-Gln; potent inhibitor, competitive and non-competitive inhibition with respect to ATP and XMP
GMP
-
0.33 mM, 50% inhibition
GMP
-
competitive versus XMP, uncompetitive versus ATP, non-competitive versus L-Gln; potent inhibitor, competitive and uncompetitive inhibition with respect to XMP and ATP
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
Pigeon
-
-
Psicofuranine
-
Psicofuranine
-
0.5 mM, 25% inhibition
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Carcinoma
Dynamic compartmentalization of purine nucleotide metabolic enzymes at leading edge in highly motile renal cell carcinoma.
Carcinoma, Hepatocellular
Biochemical pharmacology of acivicin in rat hepatoma cells.
Carcinoma, Hepatocellular
Enzymes of purine metabolism in cancer.
Carcinoma, Hepatocellular
Guanosine-5'-phosphate synthetase and guanosine-5'-phosphate kinase in rat hepatomas and kidney tumors.
Carcinoma, Hepatocellular
Inactivation by acivicin of rat brain CTP and GMP synthetases and depression of CTP and GTP concentrations.
Carcinoma, Hepatocellular
Methotrexate decreases thymidine kinase activity.
Carcinoma, Hepatocellular
Oncolytic activity and mechanism of action of a novel L-cysteine derivative, L-cysteine, ethyl ester, S-(N-methylcarbamate) monohydrochloride.
Carcinoma, Hepatocellular
Recovery of the activities of IMP dehydrogenase and GMP synthase after treatment with tiazofurin and acivicin in hepatoma cells in vitro.
Carcinoma, Renal Cell
Dynamic compartmentalization of purine nucleotide metabolic enzymes at leading edge in highly motile renal cell carcinoma.
Dehydration
Intra-specific variations in expression of stress-related genes in beech progenies are stronger than drought-induced responses.
Infections
GMP Synthase Is Required for Virulence Factor Production and Infection by Cryptococcus neoformans.
Inflammatory Bowel Diseases
Nonsynonymous Polymorphism in Guanine Monophosphate Synthetase Is a Risk Factor for Unfavorable Thiopurine Metabolite Ratios in Patients With Inflammatory Bowel Disease.
Insulin Resistance
Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance.
Leukemia
Mechanism of resistance of a variant of P388 leukemia to L-(alpha S,5S)-alpha-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid (acivicin).
Liver Neoplasms
Proteomic Analysis Reveals GMP Synthetase as p53 Repression Target in Liver Cancer.
Mycoses
GMP Synthase Is Required for Virulence Factor Production and Infection by Cryptococcus neoformans.
Neoplasms
Guanosine-5'-phosphate synthetase and guanosine-5'-phosphate kinase in rat hepatomas and kidney tumors.
Neoplasms
Mycophenolic acid and its mechanism of action in cancer and psoriasis.
Neoplasms
Oncolytic activity and mechanism of action of a novel L-cysteine derivative, L-cysteine, ethyl ester, S-(N-methylcarbamate) monohydrochloride.
Neoplasms
Quantification of Isotope Encoded Proteins in 2-D Gels Using Surface Enhanced Resonance Raman.
Neoplasms
Regulation of GTP biosynthesis.
Neoplasms
Targets and markers of selective action of tiazofurin.
Prostatic Neoplasms
Inhibition of guanosine monophosphate synthetase (GMPS) blocks glutamine metabolism and prostate cancer growth.
Sarcoma, Yoshida
Purification and characterization of GMP synthetase from Yoshida sarcoma ascites cells.
Starvation
DegS-DegU and ComP-ComA modulator-effector pairs control expression of the Bacillus subtilis pleiotropic regulatory gene degQ.
Starvation
Expression of kinA and kinB of Bacillus subtilis, Necessary for Sporulation Initiation, Is under Positive Stringent Transcription Control.
Starvation
Guanosine-5'-phosphate synthetase and guanosine-5'-phosphate kinase in rat hepatomas and kidney tumors.
Tuberculosis
Biochemical characterization of recombinant guaA-encoded guanosine monophosphate synthetase (EC 6.3.5.2) from Mycobacterium tuberculosis H37Rv strain.
Tuberculosis
Characterization of the D-xylulose 5-phosphate/D-fructose 6-phosphate phosphoketolase gene (xfp) from Bifidobacterium lactis.
Tuberculosis
Glutamine amidotransferase activity of NAD+ synthetase from Mycobacterium tuberculosis depends on an amino-terminal nitrilase domain.
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Hirai, K.; Matsuda, Y.; Nakagawa, H.
Purification and characterization of GMP synthetase from Yoshida sarcoma ascites cells
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1987
Rattus norvegicus
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Construction of a plasmid for high level expression of XMP aminase in Escherichia coli
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Escherichia coli
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Zalkin, H.
GMP synthetase
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Escherichia coli, Escherichia coli B96
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Nucleotide sequence of the guaA gene encoding GMP synthetase of Escherichia coli K12
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GMP synthetase from Ehrlich ascites cells
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GMP synthetase (Escherichia coli)
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Escherichia coli, Escherichia coli B96
brenda
Spector, T.; Jones, T.E.; Krenitsky, T.A.; Harvey, R.J.
Guanosine monophosphate synthetase from Ehrlich ascites cells. Multiple inhibition by pyrophosphate and nucleosides
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GMP synthetase from Escherichia coli B-96. Interactions with substrate analogs
Biochim. Biophys. Acta
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1974
Escherichia coli, Escherichia coli B96
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Preferential utilization of glutamine for amination of xanthosine 5'-phosphate to guanosine 5'-phosphate by purified enzymes from Escherichia coli
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Escherichia coli, Escherichia coli B / ATCC 11303, Escherichia coli B96
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Escherichia coli, Escherichia coli B96
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Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA
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The glutamine hydrolysis function of human GMP synthetase. Identification of an essential active site cysteine
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High-level production from a baculovirus expression system and biochemical characterization of human GMP synthetase
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Homo sapiens
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Preliminary X-ray analysis of Escherichia coli GMP synthetase: determination of anomalous scattering factors for a cysteinyl mercury derivative
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1994
Escherichia coli
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1
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Escherichia coli
-
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Thrazarine, a new antitumor antibiotic. I. Taxonomy, fermentation, isolation and biological properties
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Genetic and physiological characterization of the purine salvage pathway in the archaebacterium Methanobacterium thermoautotrophicum Marburg
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Production of guanosine by psicofuranine and decoyinine resistant mutants of Bacillus subtilis
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-
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Properties of xanthosine 5'-monophosphate-amidotransferase from Escherichia coli
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Characterization of the glutamine site of Escherichia coli guanosine 5'-monophosphate synthetase
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Xanthosine-5'-phosphate amidotransferase from Escherichia coli
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Biosynthesis of guanosine 5'-phosphate. II. Amination of xanthosine 5'-phosphate by purified enzyme from pigeon liver
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Guanosine-5'-phosphate synthetase and guanosine-5'-phosphate kinase in rat hepatomas and kidney tumors
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1981
Rattus norvegicus
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Dujardin, G.; Kermorgant, M.; Slonimski, P.P.; Boucherie, H.
Cloning and sequencing of the GMP synthetase-encoding gene of Saccharomyces cerevisiae
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Saccharomyces cerevisiae
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Functional cloning of a Dictyostelium discoideum cDNA encoding GMP synthetase
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Dictyostelium discoideum
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Dual inhibitory effect of bredinin
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N2-hydroxyguanosine 5'-monophosphate is a time-dependent inhibitor of Escherichia coli guanosine monophosphate synthetase
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Escherichia coli
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Mechanism for acivicin inactivation of triad glutamine amidotransferases
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2001
Escherichia coli (P04079), Escherichia coli
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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
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Homo sapiens
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Genetic organization and polymorphism of the guaA gene encoding the GMP synthetase in Lactobacillus rhamnosus
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2000
Lacticaseibacillus rhamnosus (O85192), Lacticaseibacillus rhamnosus, Lacticaseibacillus rhamnosus X202 (O85192)
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Plasmodium falciparum: isolation and characterisation of a gene encoding protozoan GMP synthase
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Plasmodium falciparum (Q9U775), Plasmodium falciparum
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Adenosine is the primary precursor of all purine nucleotides in Trichomonas vaginalis
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GMP synthetase stimulates histone H2B deubiquitylation by the epigenetic silencer USP7
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2005
Drosophila sp. (in: flies)
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Kinetic and biochemical characterization of Plasmodium falciparum guanosine 5-monophosphate synthetase
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The effects of removing the GAT domain from E. coli GMP synthetase
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2006
Escherichia coli (P04079), Escherichia coli
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Jiang, L.; Zhao, J.; Guo, R.; Li, J.; Yu, L.; Xu, D.
Functional characterization and virulence study of ADE8 and GUA1 genes involved in the de novo purine biosynthesis in Candida albicans
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2010
Candida albicans, Candida albicans CAI-4
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Jewett, M.W.; Lawrence, K.A.; Bestor, A.; Byram, R.; Gherardini, F.; Rosa, P.A.
GuaA and GuaB are essential for Borrelia burgdorferi survival in the tick-mouse infection cycle
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2009
Borreliella burgdorferi
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Maruoka, S.; Horita, S.; Lee, W.C.; Nagata, K.; Tanokura, M.
Crystal structure of the ATPPase subunit and its substrate-dependent association with the GATase subunit: a novel regulatory mechanism for a two-subunit-type GMP synthetase from Pyrococcus horikoshii OT3
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van der Knaap, J.A.; Kozhevnikova, E.; Langenberg, K.; Moshkin, Y.M.; Verrijzer, C.P.
Biosynthetic enzyme GMP synthetase cooperates with ubiquitin-specific protease 7 in transcriptional regulation of ecdysteroid target genes
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Drosophila melanogaster
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Iglesias-Gato, D.; Martin-Marcos, P.; Santos, M.A.; Hinnebusch, A.G.; Tamame, M.
Guanine nucleotide pool imbalance impairs multiple steps of protein synthesis and disrupts GCN4 translational control in Saccharomyces cerevisiae
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Saccharomyces cerevisiae
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Chatterjee, S., Killiny, N., Almeida, R.P., Lindow, S.E.
Role of cyclic di-GMP in Xylella fastidiosa biofilm formation, plant virulence, and insect transmission
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Xylella fastidiosa
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Crystal structure of glutamine amidotransferase from Pyrococcus horikoshii OT3
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Biochemical characterization of recombinant guaA-encoded guanosine monophosphate synthetase (EC 6.3.5.2) from Mycobacterium tuberculosis H37Rv strain
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517
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2012
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
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Oliver, J.C.; Linger, R.S.; Chittur, S.V.; Davisson, V.J.
Substrate activation and conformational dynamics of guanosine 5'-monophosphate synthetase
Biochemistry
52
5225-5235
2013
Escherichia coli
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Ali, R.; Kumar, S.; Balaram, H.; Sarma, S.P.
1H, 13C, 15N assignment and secondary structure determination of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii
Biomol. NMR Assign.
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2012
Methanocaldococcus jannaschii
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Bhat, J.Y.; Venkatachala, R.; Balaram, H.
Substrate-induced conformational changes in Plasmodium falciparum guanosine monophosphate synthetase
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278
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Plasmodium falciparum
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Substrate specificity and oligomerization of human GMP synthetase
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425
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Homo sapiens (P49915), Homo sapiens
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Oliver, J.C.; Gudihal, R.; Burgner, J.W.; Pedley, A.M.; Zwierko, A.T.; Davisson, V.J.; Linger, R.S.
Conformational changes involving ammonia tunnel formation and allosteric control in GMP synthetase
Arch. Biochem. Biophys.
545
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2014
Escherichia coli (P04079)
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