BRENDA - Enzyme Database show
show all sequences of 6.3.3.1

Purification and characterization of aminoimidazole ribonucleotide synthetase from Escherichia coli

Schrimsher, J.L.; Schendel, F.J.; Stubbe, J.; Smith, J.M.; Biochemistry 25, 4366-4371 (1986)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
1-(5-phosphoribosyl)-5-aminoimidazole
-
Escherichia coli
ADP
-
Escherichia coli
phosphate
-
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.027
-
2-(formamido)-N1-(5-phosphoribosyl)acetamidine
-
Escherichia coli
0.065
-
MgATP2-
-
Escherichia coli
0.172
-
ATPgammaS
-
Escherichia coli
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
K+
absolutely required; Km: 96 mM
Escherichia coli
Mg2+
absolutely required; Km: 0.3 mM
Escherichia coli
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
38500
-
2 * 38500, SDS-PAGE
Escherichia coli
71700
-
gel filtration, sucrose density gradient ultracentrifugation
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
Escherichia coli
fifth step in de novo purine biosynthesis
?
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
Escherichia coli
enzyme of purine biosynthetic pathway
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Purification (Commentary)
Commentary
Organism
-
Escherichia coli
Reaction
Reaction
Commentary
Organism
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; sequential mechanism in which ATP binds first to the enzyme and ADP is released last
Escherichia coli
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
3.35
-
-
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
-
1308
Escherichia coli
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
-
1308
Escherichia coli
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
fifth step in de novo purine biosynthesis
1308
Escherichia coli
?
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
enzyme of purine biosynthetic pathway
1308
Escherichia coli
?
-
-
-
-
ATPgammaS + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
-
1308
Escherichia coli
ADP + ? + 1-(5-phosphoribosyl)-5-aminoimidazole
-
-
-
-
Subunits
Subunits
Commentary
Organism
dimer
2 * 38500, SDS-PAGE
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
-
Escherichia coli
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1-(5-phosphoribosyl)-5-aminoimidazole
-
Escherichia coli
ADP
-
Escherichia coli
phosphate
-
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.027
-
2-(formamido)-N1-(5-phosphoribosyl)acetamidine
-
Escherichia coli
0.065
-
MgATP2-
-
Escherichia coli
0.172
-
ATPgammaS
-
Escherichia coli
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
K+
absolutely required; Km: 96 mM
Escherichia coli
Mg2+
absolutely required; Km: 0.3 mM
Escherichia coli
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
38500
-
2 * 38500, SDS-PAGE
Escherichia coli
71700
-
gel filtration, sucrose density gradient ultracentrifugation
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
Escherichia coli
fifth step in de novo purine biosynthesis
?
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
Escherichia coli
enzyme of purine biosynthetic pathway
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Escherichia coli
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
3.35
-
-
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
-
1308
Escherichia coli
ADP + phosphate + 1-(5-phosphoribosyl)-5-aminoimidazole
-
1308
Escherichia coli
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
fifth step in de novo purine biosynthesis
1308
Escherichia coli
?
-
-
-
-
ATP + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
enzyme of purine biosynthetic pathway
1308
Escherichia coli
?
-
-
-
-
ATPgammaS + 2-(formamido)-N1-(5-phosphoribosyl)acetamidine
-
1308
Escherichia coli
ADP + ? + 1-(5-phosphoribosyl)-5-aminoimidazole
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 38500, SDS-PAGE
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
-
Escherichia coli
Other publictions for EC 6.3.3.1
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
745399
Rao
Identification of potential i ...
Pyrococcus horikoshii, Pyrococcus horikoshii OT-3
J. Biomol. Struct. Dyn.
34
2199-2213
2016
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653535
Goggin
Dual intracellular localizatio ...
Vigna unguiculata
Plant Physiol.
131
1033-1041
2003
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651681
Zilles
Altered pathway routing in a c ...
Salmonella enterica
J. Bacteriol.
183
2234-2240
2001
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649909
Mueller
Investigation of the ATP Bindi ...
Escherichia coli
Biochemistry
38
9831-9839
1999
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1
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653485
Smith
AIR synthetase in cowpea nodul ...
Vigna unguiculata
Plant Mol. Biol.
36
811-820
1998
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1
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653875
Dutova
-
Genetic control of purine bios ...
Ogataea methanolica
Russ. J. Genet.
34
43-50
1998
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1316
Tret'iakov
Glycine amide ribonucleotide s ...
Saccharomyces cerevisiae
Biokhimiia
60
2011-2021
1995
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1317
Senecoff
Isolating the Arabidopsis thal ...
Arabidopsis thaliana
Plant Physiol.
102
387-399
1993
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1318
Chang
Expression of a human cDNA enc ...
Homo sapiens
Somat. Cell Mol. Genet.
17
411-420
1991
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1306
Saxild
Gene-enzyme relationships of t ...
Bacillus subtilis
Mol. Gen. Genet.
211
160-167
1988
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1259
Ebbole
Cloning and characterization o ...
Bacillus subtilis
J. Biol. Chem.
262
8274-8287
1987
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1307
Smith
Nucleotide sequence of the pur ...
Escherichia coli
J. Biol. Chem.
261
10632-10636
1986
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1308
Schrimsher
Purification and characterizat ...
Escherichia coli
Biochemistry
25
4366-4371
1986
-
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3
3
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2
2
2
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2
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1
1
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4
1
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1
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3
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2
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1
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1
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4
1
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1
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1309
Schrimsher
Isolation of a multifunctional ...
Gallus gallus
Biochemistry
25
4356-4365
1986
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2
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2
2
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2
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1
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1
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1
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1
1
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1310
Daubner
Structural and mechanistic stu ...
Gallus gallus, Homo sapiens
Biochemistry
25
2951-2957
1986
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1311
Henikoff
Multiple purine pathway enzyme ...
Drosophila melanogaster
Proc. Natl. Acad. Sci. USA
83
720-724
1986
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1312
Daubner
A multifunctional protein poss ...
Gallus gallus
Biochemistry
24
7059-7062
1985
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1
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1313
Fluri
The product of the ade1 gene i ...
Schizosaccharomyces pombe
Mol. Gen. Genet.
147
271-282
1976
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2
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2
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1
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1
1
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1315
Levenberg
-
Biosynthesis of the purines. X ...
Pigeon
J. Biol. Chem.
224
1018-1027
1957
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