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5'-phosphoribosylformylglycinamide + ATP + L-glutamine + H2O
phosphoribosylformylglycinamidine + L-glutamate + ADP + phosphate
5'-phosphoribosylformylglycinamide + L-glutamine + ATP
phosphoribosylformylglycinamidine + L-glutamate + ADP + phosphate
ATP + 5'-phosphoribosylformylglycinamide + L-Gln
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
ATP + 5'-phosphoribosylformylglycinamide + NH4+ + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine
ATP + carbocyclic-5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + carbocyclic-5'-phosphoribosylformylglycinamidine + L-Glu
-
(+/-)carbocyclic-5'-phosphoribosylformylglycinamide and (-)5'-phosphoribosylformylglycinamide at 10% of the activity relative to 5'-phosphoribosylformylglycinamide
-
-
?
ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O
ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate
formylglycinamide ribonucleotide + ATP + L-glutamine + H2O
formylglycinamidine ribonucleotide + ADP + phosphate + L-glutamate
formylglycinamide ribonucleotide + ATP + NH3 + H2O
formylglycinamidine ribonucleotide + ADP + phosphate
-
-
-
-
?
additional information
?
-
5'-phosphoribosylformylglycinamide + ATP + L-glutamine + H2O
phosphoribosylformylglycinamidine + L-glutamate + ADP + phosphate
-
-
-
?
5'-phosphoribosylformylglycinamide + ATP + L-glutamine + H2O
phosphoribosylformylglycinamidine + L-glutamate + ADP + phosphate
-
-
-
?
5'-phosphoribosylformylglycinamide + L-glutamine + ATP
phosphoribosylformylglycinamidine + L-glutamate + ADP + phosphate
-
-
-
r
5'-phosphoribosylformylglycinamide + L-glutamine + ATP
phosphoribosylformylglycinamidine + L-glutamate + ADP + phosphate
-
fourth step in the de novo purine biosynthetic pathway
-
r
ATP + 5'-phosphoribosylformylglycinamide + L-Gln
?
-
enzyme of de novo purine nucleotide synthesis
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln
?
-
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
Pigeon
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + L-Gln + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine + L-Glu
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + NH4+ + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine
-
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + NH4+ + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine
-
-
-
-
?
ATP + 5'-phosphoribosylformylglycinamide + NH4+ + H2O
ADP + phosphate + 5'-phosphoribosylformylglycinamidine
-
-
-
-
?
ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O
ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate
-
-
-
-
?
ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O
ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate
-
ATP in form of MgATP2-
-
-
?
ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O
ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate
-
-
-
?
ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O
ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate
fourth step of the purine biosynthetic pathway
-
-
?
ATP + N2-formyl-N1-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O
ADP + phosphate + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine + L-glutamate
-
fourth step of the purine biosynthetic pathway
-
-
?
formylglycinamide ribonucleotide + ATP + L-glutamine + H2O
formylglycinamidine ribonucleotide + ADP + phosphate + L-glutamate
-
-
-
-
?
formylglycinamide ribonucleotide + ATP + L-glutamine + H2O
formylglycinamidine ribonucleotide + ADP + phosphate + L-glutamate
-
-
-
-
?
formylglycinamide ribonucleotide + ATP + L-glutamine + H2O
formylglycinamidine ribonucleotide + ADP + phosphate + L-glutamate
-
fourth step of purine biosynthetic pathway
-
-
?
additional information
?
-
-
fourth step in purine biosynthesis
-
?
additional information
?
-
-
glutamyl derivatives, e.g. gamma-glutamylhydroxamate, gamma-glutamyl hydrazine, gamma-glutamyl esters, and gamma-glutamyl thioesters are hydrolyzed with strict dependence on Mg2+, ATP, and 5'-phosphoribosylformylglycinamide
-
-
?
additional information
?
-
Murine gammaherpesvirus-68
virion tegument protein ORF75c is essential for production of infectious virus.ORF75c induces the rapid degradation of promyelocytic leukemia nuclear body by a proteasome-dependent mechanism and loss of promyelocytic leukemia nuclear body correlates with more robust viral replication. Phosphoribosylformylglycinamidine synthase activity is inferred from electronic annotation
-
-
?
additional information
?
-
-
purine biosynthesis
-
?
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Carcinoma
Proliferation-linked increase in phosphoribosylformylglycinamidine synthetase activity (EC 6.3.5.3).
Carcinoma, Hepatocellular
In vivo inactivation of formylglycinamidine ribonucleotide synthetase in rat hepatoma.
Carcinoma, Hepatocellular
Oncolytic activity and mechanism of action of a novel L-cysteine derivative, L-cysteine, ethyl ester, S-(N-methylcarbamate) monohydrochloride.
Carcinoma, Hepatocellular
Proliferation-linked increase in phosphoribosylformylglycinamidine synthetase activity (EC 6.3.5.3).
Carcinoma, Renal Cell
Proliferation-linked increase in phosphoribosylformylglycinamidine synthetase activity (EC 6.3.5.3).
Herpes Simplex
Expression of the purine biosynthetic enzyme phosphoribosyl formylglycinamidine synthase in neurons.
Infections
Correction: Viral FGARAT ORF75A promotes early events in lytic infection and gammaherpesvirus pathogenesis in mice.
Infections
Multiple functions for ORF75c in murid herpesvirus-4 infection.
Infections
Murine gammaherpesvirus 68 encodes a second PML-modifying protein.
Infections
Viral FGARAT ORF75A promotes early events in lytic infection and gammaherpesvirus pathogenesis in mice.
Leukemia
Murine gammaherpesvirus 68 encodes a second PML-modifying protein.
Leukemia
Murine gammaherpesvirus 68 ORF75c contains ubiquitin E3 ligase activity and requires PML SUMOylation but not other known cellular PML regulators, CK2 and E6AP, to mediate PML degradation.
Neoplasms
Oncolytic activity and mechanism of action of a novel L-cysteine derivative, L-cysteine, ethyl ester, S-(N-methylcarbamate) monohydrochloride.
Neoplasms
Proliferation-linked increase in phosphoribosylformylglycinamidine synthetase activity (EC 6.3.5.3).
Neuroblastoma
Expression of the purine biosynthetic enzyme phosphoribosyl formylglycinamidine synthase in neurons.
Protein Deficiency
Human phosphoribosylformylglycineamide amidotransferase (FGARAT): regional mapping, complete coding sequence, isolation of a functional genomic clone, and DNA sequence analysis.
Virus Diseases
Expression of the purine biosynthetic enzyme phosphoribosyl formylglycinamidine synthase in neurons.
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determination of structure of PurS in two different crystal forms P2(1) and C2 at 2.5 and 2.0 A resolution, respectively. PurS forms a tight dimer with a central six-stranded beta-sheet flanked by four helices. In both the P2(1) and the C2 crystal forms, the quaternary structure of PurS is a tetramer. Native PurS is crystallized from 2.0 M ammonium sulfate, 6% PEG 400, 100 mM HEPES, pH 7.3. The crystals are grown at room temperature using the hanging-drop vapor diffusion technique. Drops containing a 2:1 mixture of protein and reservoir solution are optimal for crystal growth. Crystals grow over a period of 4-7 days. Under these conditions, PurS crystallizes in the monoclinic space group P2(1) with unit cell dimensions a = 42.91 A, b = 87.96 A, c = 52.68 A, and beta = 94.97°. The SeMet-PurS crystals grow in 20% PEG 4K, 5% glycerol, 15% 2-propanol, 100 mM sodium citrate, pH 5.6. Optimal drop size is 0.004 mL using a 1:1 mixture of protein and reservoir. Under these conditions, the protein crystallizes in the space group C2 with unit cell dimensions a = 89.13 A, b = 42.21 A, c = 47.03 A, and beta = 118.22°
-
to 2.3 A resolution. Molecular dynamics simulation and comparison with PurS from Thermus thermophilus and Methanocaldococcus jannaschii
crucial component MTH169, space group P4(3)22, unit cell parameters a : 53.8 A, c : 142.7 A
-
algorithm RismPath which enables fast and accurate determination of solvent distribution inside a protein channel, predicts an auxiliary ADP-adjacent path as the preferred mode of ammonia transfer. The residues in the middle of the channel do not partake in catalytic coupling and serve only as channel walls facilitating ammonia transfer
crystals of the pure SeMet-enzyme are grown at room temperature using hanging-drop vapor diffusion method. StPurL crystallizes in the hexagonal space group P6(5) with unit cell dimensions of a = 145.3 and c = 140.9 A. The asymmetric unit contains one monomer, corresponding to calculated solvent content of 57%. Domain organization revealed by X-ray crystallography
-
mutants R1263A and F209W, vapor diffusion method
to 1.55 A resolution. Molecular dynamics simulation and comparison with PurS from Thermus thermophilus and Methanocaldococcus jannaschii
crystal structure of phosphoribosylformyl-glycinamidine synthase II, PurS subunit (TM1244) at 1.90 A resolution
hanging drop method, enzyme in complex with formylglycinamide ribonucleotide, mutant enzyme H72A in complex with beta,gamma-methylene adenosine 5'-triphosphate, mutant enzyme H72A in complex with ADP, enzyme in complex with formylglycinamide ribonucleotide and beta,gamma-methylene adenosine 5'-triphosphate, enzyme in complex with ATP
in complex with gene products PurQ and PurS, to 3.5 A resolution. The complex has a stoichiometry of 2:1:1 for components PurS:PurQ:PurL, respectively. The flexibility of the PurS dimer is involved in the activation of the complex and the formation of an ammonia channel
nanodroplet vapor diffusion method, crystal structure of phosphoribosylformylglycinamidine synthase II (smPurL) from Thermotoga maritima at 2.15 A resolution
to 1.64 A resolution. Molecular dynamics simulation and comparison with PurS from Sulfolobus tokodaii and Methanocaldococcus jannaschii
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Ebbole, D.J.; Zalkin, H.
Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis
J. Biol. Chem.
262
8274-8287
1987
Bacillus subtilis
brenda
Caperelli, C.A.; Liu, D.
Carbocyclic substrates for de novo purine biosynthesis. Enantiospecific synthesis and enantiospecificity of enzymatic utilization
J. Biol. Chem.
267
9783-9787
1992
Escherichia coli
brenda
Schendel, F.J.; Stubbe, J.
Substrate specificity of formylglycinamide synthetase
Biochemistry
25
2256-2264
1986
Gallus gallus
brenda
Elliott, W.L.; Weber, G.
Proliferation-linked increase in phosphoribosylformylglycinamidine synthetase activity
Cancer Res.
44
2430-2434
1984
Homo sapiens, Rattus norvegicus
brenda
Buchanan, J.M.
Covalent reaction of substrates and antimetabolites with formylglycinamide ribonucleotide amidotransferase
Methods Enzymol.
87
76-84
1982
Gallus gallus, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Buchanan, J.M.; Ohnoki, S.; Hong, B.S.
2-Formamido-N-ribosylacetamide 5'-phosphate:L-glutamine amido-ligase (adenosine diphosphate)
Methods Enzymol.
51
193-201
1978
Gallus gallus, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Buchanan, J.M.
The Amidotransferases
Adv. Enzymol. Relat. Areas Mol. Biol.
39
91-183
1973
Gallus gallus, Mus musculus, Pigeon, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Chu, S.Y.; Henderson, J.F.
Kinetic studies of phosphoribosyl-formylglycinamidine synthetase
Can. J. Biochem.
50
490-500
1972
Mus musculus
brenda
Chu, S.Y.; Henderson, J.F.
Purification and properties of phosphoribosyl-formylglycinamidine synthetase of Ehrlich ascites tumor cells
Can. J. Biochem.
50
484-489
1972
Mus musculus
brenda
Schendel, F.J.; Mueller, E.; Stubbe, J.
Formylglycinamide ribonucleotide synthetase from Escherichia coli: cloning, sequencing, overproduction, isolation, and characterization
Biochemistry
28
2459-2471
1989
Escherichia coli
brenda
Saxild, H.H.; Nygaard, P.
The yexA gene product is required for phosphoribosylformylglycinamidine synthetase activity in Bacillus subtilis
Microbiology
146
807-814
2000
Bacillus subtilis
brenda
Batra, R.; Christendat, D.; Edwards, A.; Arrowsmith, C.; Tong, L.
Crystal structure of MTH169, a crucial component of phosphoribosylformylglycinamidine synthetase
Proteins Struct. Funct. Genet.
49
285-288
2002
Methanothermobacter thermautotrophicus
brenda
Dutova, T.A.; Tarutina, M.G.; Milgrom, E.M.; Serkova, N.N.; Tolstorukov, I.I.
Genetic control of purine biosynthesis in yeast Pichia methanolica. The ADE5 (PUR4) gene controlling 5'-phosphoribosylformyl glycinamidine synthetase
Russ. J. Genet.
36
1375-1384
2000
Ogataea methanolica
-
brenda
Hoskins, A.A.; Anand, R.; Ealick, S.E.; Stubbe, J.
The formylglycinamide ribonucleotide amidotransferase complex from Bacillus subtilis: metabolite-mediated complex formation
Biochemistry
43
10314-10327
2004
Bacillus subtilis
brenda
Anand, R.; Hoskins, A.A.; Stubbe, J.; Ealick, S.E.
Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography
Biochemistry
43
10328-10342
2004
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Anand, R.; Hoskins, A.A.; Bennett, E.M.; Sintchak, M.D.; Stubbe, J.; Ealick, S.E.
A model for the Bacillus subtilis formylglycinamide ribonucleotide amidotransferase multiprotein complex
Biochemistry
43
10343-10352
2004
Bacillus subtilis
brenda
Morar, M.; Anand, R.; Hoskins, A.A.; Stubbe, J.; Ealick, S.E.
Complexed structures of formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima describe a novel ATP binding protein superfamily
Biochemistry
45
14880-14895
2006
Thermotoga maritima (Q9X0X3), Thermotoga maritima
brenda
Ambing, E.; Canaves, J.M.; Chiu, H.; Deacon, A.M.; DiDonato, M.; Elsliger, M.; Godzik, A.; Grittini, C.; Grzechnik, S.K.; Hale, J.; Hampton, E.; Han, G.W.; Haugen, J.; Jaroszewski, L.; Klock, H.E.; Koesema, E.; Kreusch, A.; Kuhn, P.; Lesley, S.A.; Levin, I.; Miller, M.D.; Moy, K.; Nigoghossian, E.; Paulsen, J.; Quijano, K.; Reyes, R.; Spraggon, G.; Stevens, R.C.; van den Bedem, H.; Velasquez, J.; White, A.; Wolf, G.; Xu, Q.; Hodgson, K.O.; Wooley, J.; Wilson, I. A.
Crystal structure of phosphoribosylformylglycinamidine synthase II (smPurL) from Thermotoga maritima at 2.15 A resolution
Proteins Struct. Funct. Bioinform.
63
1106-1111
2006
Thermotoga maritima (Q9X0X3), Thermotoga maritima
brenda
Mathews, I.I.; Krishna, S.S.; Schwarzenbacher, R.; McMullan, D.; Jaroszewski, L.; Miller, M.D.; Abdubek, P.; Agarwalla, S.; Ambing, E.; Axelrod, H.L.; Canaves, J.M.; Carlton, D.; Chiu, H.; Clayton, T.; DiDonato, M.; Duan, L.; Elsliger, M.; Grzechnik, S.K.
Crystal structure of phosphoribosylformyl-glycinamidine synthase II, PurS subunit (TM1244) from Thermotoga maritima at 1.90 A resolution
Proteins Struct. Funct. Bioinform.
65
249-254
2006
Thermotoga maritima (Q9X0X1)
brenda
Morar, M.; Hoskins, A.A.; Stubbe, J.; Ealick, S.E.
Formylglycinamide ribonucleotide amidotransferase from Thermotoga maritima: structural insights into complex formation
Biochemistry
47
7816-7830
2008
Thermotoga maritima (Q9X0X3), Thermotoga maritima
brenda
Ling, P.D.; Tan, J.; Sewatanon, J.; Peng, R.
Murine gammaherpesvirus 68 open reading frame 75c tegument protein induces the degradation of PML and is essential for production of infectious virus
J. Virol.
82
8000-8012
2008
Murine gammaherpesvirus-68 (O41976)
brenda
Berthome, R.; Thomasset, M.; Maene, M.; Bourgeois, N.; Froger, N.; Budar, F.
pur4 Mutations are lethal to the male, but not the female, gametophyte and affect sporophyte development in Arabidopsis
Plant Physiol.
147
650-660
2008
Arabidopsis thaliana
brenda
Tanwar, A.S.; Goyal, V.D.; Choudhary, D.; Panjikar, S.; Anand, R.
Importance of hydrophobic cavities in allosteric regulation of formylglycinamide synthetase: insight from xenon trapping and statistical coupling analysis
PLoS ONE
8
e77781
2013
Salmonella enterica subsp. enterica serovar Typhimurium (P74881)
brenda
Tanwar, A.S.; Sindhikara, D.J.; Hirata, F.; Anand, R.
Determination of the formylglycinamide ribonucleotide amidotransferase ammonia pathway by combining 3D-RISM theory with experiment
ACS Chem. Biol.
10
698-704
2015
Salmonella enterica subsp. enterica serovar Typhimurium (P74881)
brenda
Watanabe, Y.; Yanai, H.; Kanagawa, M.; Suzuki, S.; Tamura, S.; Okada, K.; Baba, S.; Kumasaka, T.; Agari, Y.; Chen, L.; Fu, Z.; Chrzas, J.; Wang, B.; Nakagawa, N.; Ebihara, A.; Masui, R.; Kuramitsu, S.; Yokoyama, S.; Sampei, G.; Kawai, G.
Crystal structures of a subunit of the formyl-glycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii
Acta Crystallogr. Sect. F
72
627-635
2016
Methanocaldococcus jannaschii (Q58988), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58988), Sulfurisphaera tokodaii (F9VNF4), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (F9VNF4), Thermus thermophilus (Q5SI58), Thermus thermophilus, Thermus thermophilus DSM 579 (Q5SI58)
brenda
Mangold, C.A.; Yao, P.J.; Du, M.; Freeman, W.M.; Benkovic, S.J.; Szpara, M.L.
Expression of the purine biosynthetic enzyme phosphoribosyl formylglycinamidine synthase (FGAMS) in neurons
J. Neurochem.
144
723-735
2018
Homo sapiens (O15067), Homo sapiens, Rattus norvegicus
brenda