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Information on EC 6.3.3.1 - phosphoribosylformylglycinamidine cyclo-ligase
for references in articles please use BRENDA:EC6.3.3.1
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EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.3 Cyclo-ligases
6.3.3.1 phosphoribosylformylglycinamidine cyclo-ligase
The enzyme appears in viruses and cellular organisms
- 6.3.3.1
- purine
-
transformylase
- glycinamide
-
trifunctional
-
phosphoribosylglycinamide
-
formyltransferase
-
monofunctional
-
amidotransferase
-
formylglycinamide
-
2.1.2.2
- cowpea
-
purl
-
phosphoribosylamine
- unguiculata
Reaction Schemes
showSynonyms
air synthetase, aminoimidazole ribonucleotide synthetase, phosphoribosylaminoimidazole synthetase, phosphoribosylformylglycinamidine cyclo-ligase, phosphoribosyl-aminoimidazole synthetase, 5'-phosphoribosyl-5-aminoimidazole synthetase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-Aminoimidazole ribonucleotide synthetase
-
-
-
-
5'-Phosphoribosyl-5-aminoimidazole synthetase
-
-
-
-
AIR synthase
-
-
-
-
AIR synthetase
-
-
-
-
AIRS
aminoimidazole ribonucleotide synthetase
Phosphoribosyl-aminoimidazole synthetase
-
-
-
-
Phosphoribosylaminoimidazole synthetase
-
-
-
-
PurM
Synthetase, phosphoribosylaminoimidazole
-
-
-
-
AIRS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
enzyme catalyzes transfer of the oxygen of the formyl group to phosphate
-
ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
mechanism
-
ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
mechanism
-
ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
sequential mechanism in which ATP binds first to the enzyme and ADP is released last
-
ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
5-aminoimidazole ribonucleotide biosynthesis I, 5-aminoimidazole ribonucleotide biosynthesis II, superpathway of 5-aminoimidazole ribonucleotide biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
2-(Formamido)-N1-(5-phosphoribosyl)acetamidine cyclo-ligase (ADP-forming)
-
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CAS REGISTRY NUMBER
COMMENTARY
9023-53-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine
ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
ATPgammaS + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + ? + 1-(5-phosphoribosyl)-5-aminoimidazole
-
Substrates: -
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine
ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
-
Substrates: ATP in form of MgATP2-
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine
ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole
-
Substrates: ATP in form of MgATP2-
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
-
Substrates: enzyme of purine biosynthetic pathway
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
-
Substrates: enzyme of purine biosynthetic pathway
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
-
Substrates: fifth step in de novo purine biosynthesis
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
-
Substrates: enzyme of purine biosynthetic pathway
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
Pigeon
-
Substrates: enzyme of purine biosynthetic pathway
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
-
Substrates: -
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
-
Substrates: -
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
-
Substrates: -
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
-
Substrates: -
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
Substrates: -
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
-
Substrates: -
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
-
Substrates: ir
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
-
Substrates: -
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
-
Substrates: -
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
Pigeon
-
Substrates: -
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
-
Substrates: -
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
Substrates: -
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
-
Substrates: -
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
Substrates: -
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
-
Substrates: -
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
-
Substrates: enzyme of purine biosynthetic pathway
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
-
Substrates: enzyme of purine biosynthetic pathway
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
-
Substrates: fifth step in de novo purine biosynthesis
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
-
Substrates: enzyme of purine biosynthetic pathway
Products: -
Products: -
?
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
?
Pigeon
-
Substrates: enzyme of purine biosynthetic pathway
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,3S,4R,5R)-2-(aminomethyl)-5-(hydroxymethyl)oxolane-3,4-diol
i.e. NCI_121957. Molecular docking, compound interacts with residues Lys35, Thr14, Gly136, Glu137 and Asp103, best inhibitor identified
fluorosulfonylbenzoyl adenosine
FSBA, time-dependent inactivation by covalent binding to Lys27
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Lymphoma
Mammalian glycinamide ribonucleotide transformylase. Kinetic mechanism and associated de novo purine biosynthetic activities.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.049
2-(formamido)-N1-(5-phosphoribosyl)acetamidine
37°C, pH 7.7, wild type enzyme
0.066
2-(formamido)-N1-(5-phosphoribosyl)acetamidine
37°C, pH 7.7, R35C/E57G mutant enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
overproduces a large protein with AIR synthetase activity, phosphoribosylglycinamide synthetase activity, and phosphoribosylglycinamide transformylase activity
-
-
brenda
bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
-
-
brenda
bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
-
-
brenda
trifunctional enzyme with AIR synthetase activity, phosphoribosylglycinamide synthetase activity, and phosphoribosylglycinamide transformylase activity
-
-
brenda
trifunctional enzyme with AIR synthetase activity, phosphoribosylglycinamide synthetase activity, and phosphoribosylglycinamide transformylase activity
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (22928 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
133000
-
sucrose density gradient ultracentrifugation, trifunctional enzyme: AIR synthase, glycinamide ribonucleotide synthetase, and glycinamide ribonucleotide transformylase
240000
-
gel filtration, bifunctional enzyme with AIR synthetase activity and phosphoribosylglycinamide synthetase activity
330000
-
gel filtration, trifunctional enzyme: aminoimidazole ribonucleotide synthase, glycinamide ribonucleotide synthetase, and glycineamide ribonucleotide transformylase
36400
-
2 * 36400, SDS-PAGE of the plastid enzyme, 2 * 36900, SDS-PAGE of the mitochondrial enzyme
36900
-
2 * 36400, SDS-PAGE of the plastid enzyme, 2 * 36900, SDS-PAGE of the mitochondrial enzyme
40000
-
4-6 * 40000, SDS-PAGE, bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity. Phosphoribosyl-glycinamide synthetase activity is associated with both the monomeric and multimeric forms, but AIR synthetase is only associated with the multimer
87000
-
2 * 87000, bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
?
-
4-6 * 40000, SDS-PAGE, bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity. Phosphoribosyl-glycinamide synthetase activity is associated with both the monomeric and multimeric forms, but AIR synthetase is only associated with the multimer
dimer
-
2 * 87000, bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
dimer
-
2 * 36400, SDS-PAGE of the plastid enzyme, 2 * 36900, SDS-PAGE of the mitochondrial enzyme
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling based on Escherichia coli crystal structure, and molecular dynamics simulation. The binding pocket is composed of residues Lys13, Thr14, Ala17, Leu18, Ile21, Arg26, Lys35, Glu38, Pro39, Glu40, Asp103, Leu105, Ile133, Gly135, Gly136, Gln137 and Thr138
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K27L
obtained by site-directed mutagenesis and expression in Escherichia coli
K27Q
obtained by site-directed mutagenesis and expression in Escherichia coli
K27R
obtained by site-directed mutagenesis and expression in Escherichia coli
additional information
additional information
triple mutant R35C/E57G/R198W obtained by site-directed mutagenesis
additional information
double mutant R35C/E57G obtained by site-directed mutagenesis
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
copurification of AIR synthetase, glycinamide ribonucleotide synthetase, and glycinamide ribonucleotide transformylase
-
purification of a histidine-tagged enzyme by nickel-affinity column chromatography
purification of a histidine-tagged recombinant enzyme by affinity chromatography
purification of wild type and recombinant enzymes using C8-linked ATP affinity column
trifunctional enzyme with AIR synthetase activity, phosphoribosylglycinamide synthetase activity, and phosphoribosylglycinamide transformylase activity
-
using a recombinant histidine-tagged AIRS:cyanogen bromide Sepharose affinity resin
-
bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
-
bifunctional enzyme with AIR synthetase activity and phosphoribosyl-glycinamide synthetase activity
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and characterization of a 12-gene cluster encoding nine enzymes for de novo purine nucleotide synthesis. The cluster is likely an operon and is organized into three groups of overlapping genes followed by the last gene: purEKB-purC(or)QLF-purMNH(J)-purD
-
expression in Escherichia coli of a histidine-tagged recombinant enzyme
expression of the trifunctional enzyme with AIR synthetase activity, phosphoribosylglycinamide synthetase activity, and phosphoribosylglycinamide transformylase activity, in mutant CHO cells
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Saxild, H.H.; Nygaard, P.
Gene-enzyme relationships of the purine biosynthetic pathway in Bacillus subtilis
Mol. Gen. Genet.
211
160-167
1988
Bacillus subtilis
brenda
Smith, J.M.; Daum III, H.A.
Nucleotide sequence of the purM gene encoding 5'-phosphoribosyl-5-aminoimidazole synthetase of Escherichia coli K12
J. Biol. Chem.
261
10632-10636
1986
Escherichia coli
brenda
Schrimsher, J.L.; Schendel, F.J.; Stubbe, J.; Smith, J.M.
Purification and characterization of aminoimidazole ribonucleotide synthetase from Escherichia coli
Biochemistry
25
4366-4371
1986
Escherichia coli
brenda
Schrimsher, J.L.; Schendel, F.J.; Stubbe, J.
Isolation of a multifunctional protein with aminoimidazole ribonucleotide synthetase, glycinamide ribonucleotide synthetase, and glycinamide ribonucleotide transformylase activities: characterization of aminoimidazole ribonucleotide synthetase
Biochemistry
25
4356-4365
1986
Gallus gallus
brenda
Daubner, S.C.; Young, M.; Sammons, R.D.; Courtney, L.F.; Benkovic, S.J.
Structural and mechanistic studies on the HeLa and chicken liver proteins that catalyze glycinamide ribonucleotide synthesis and formylation and aminoimidazole ribonucleotide synthesis
Biochemistry
25
2951-2957
1986
Gallus gallus, Homo sapiens
brenda
Henikoff, S.; Keene, M.A.; Sloan, J.S.; Bleskan, J.; Hards, R.; Patterson, D.
Multiple purine pathway enzyme activities are encoded at a single genetic locus in Drosophila
Proc. Natl. Acad. Sci. USA
83
720-724
1986
Drosophila melanogaster
brenda
Daubner, S.C.; Schrimsher, J.L.; Schendel, F.J.; Young, M.; Henikoff, S.; Patterson, D.; Stubbe, J.; Benkovic, S.J.
A multifunctional protein possessing glycinamide ribonucleotide synthetase, glycinamide ribonucleotide transformylase, and aminoimidazole ribonucleotide synthetase activities in de novo purine biosynthesis
Biochemistry
24
7059-7062
1985
Gallus gallus
brenda
Fluri, R.; Coddington, A.; Flury, U.
The product of the ade1 gene in Schizosaccharomyces pombe: a bifunctional enzyme catalysing two distinct steps in purine biosynthesis
Mol. Gen. Genet.
147
271-282
1976
Schizosaccharomyces pombe
brenda
Levenberg, B.; Buchanan, J.M.
Biosynthesis of the purines. XIII. Structure, enzymatic synthesis, and metabolism of (alpha-N-formyl)-glycinamide ribotide
J. Biol. Chem.
224
1018-1027
1957
Pigeon
-
brenda
Tret'iakov, O; Ryzhova, T.A.; Velichutina, I.V.; Kostikova, T.R.; Miasnikov, A.N.; Smirnov, M.N.; Domkin, V.D.
Glycine amide ribonucleotide synthetase (EC 6.3.4.13) - is aminoimidazole ribonucleotide synthetase (EC 6.3.3.1) from Saccharomyces cerevisiae
Biokhimiia
60
2011-2021
1995
Saccharomyces cerevisiae
brenda
Senecoff, J.F.; Meagher, R.B.
Isolating the Arabidopsis thaliana genes for de novo purine synthesis by suppression of Escherichia coli mutants. I. 5'-phosphoribosyl-5-aminoimidazole synthetase
Plant Physiol.
102
387-399
1993
Arabidopsis thaliana
brenda
Chang, F.H.; Barnes, T.S.; Schild, D.; Gnirke, A.; Bleskam, J.; Patterson, D.
Expression of a human cDNA encoding a protein containing GAR synthetase, AIR synthetase, and GAR transformylase corrects the defects in mutant Chinese hamster ovary cells lacking these activities
Somat. Cell Mol. Genet.
17
411-420
1991
Homo sapiens
brenda
Mueller, E.J.; Oh, S.; Kavalerchik, E.; Kappock, T.J.; Meyer, E.; Li, C.; Ealick, S.E.; Stubbe, J.
Investigation of the ATP Binding Site of Escherichia coli Aminoimidazole Ribonucleotide Synthetase Using Affinity Labeling and Site-Directed Mutagenesis
Biochemistry
38
9831-9839
1999
Escherichia coli (P08178), Escherichia coli
brenda
Zilles, J.L.; Kappock, T.J.; Stubbe, J.; Downs, D.M.
Altered pathway routing in a class of Salmonella enterica serovar Typhimurium mutants defective in aminoimidazole ribonucleotide synthetase
J. Bacteriol.
183
2234-2240
2001
Salmonella enterica (P74883)
brenda
Smith, P.M.; Mann, A.J.; Goggin, D.E.; Atkins, C.A.
AIR synthetase in cowpea nodules: a single gene product targeted to two organelles?
Plant Mol. Biol.
36
811-820
1998
Vigna unguiculata (P52424), Vigna unguiculata
brenda
Goggin, D.E.; Lipscombe, R.; Fedorova, E.; Millar, A.H.; Mann, A.; Atkins, C.A.; Smith, P.M.C.
Dual intracellular localization and targeting of aminoimidazole ribonucleotide synthetase in cowpea
Plant Physiol.
131
1033-1041
2003
Vigna unguiculata
brenda
Dutova, T.A.; Tarutina, M.G.; Efremov, B.D.; Kostikova, T.R.; Domkin, V.D.; Tolstorukov, I.I.
Genetic control of purine biosynthesis in yeast Pichia methanolica: identification of bifunctional gene ADE7,4 controlling activity of GAR and AIR synthetases
Russ. J. Genet.
34
43-50
1998
Ogataea methanolica
-
brenda
Rao, R.G.; Biswal, J.; Dhamodharan, P.; Kanagarajan, S.; Jeyaraman, J.
Identification of potential inhibitors for AIRS from de novo purine biosynthesis pathway through molecular modeling studies - a computational approach
J. Biomol. Struct. Dyn.
34
2199-2213
2016
Pyrococcus horikoshii (O58054), Pyrococcus horikoshii, Pyrococcus horikoshii OT-3 (O58054)
brenda
EXTERNAL LINKS (specific for EC-Number 6.3.3.1)
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