BRENDA - Enzyme Database show
show all sequences of 5.4.99.18

Structural and biochemical characterization of N5-carboxyaminoimidazole ribonucleotide synthetase and N5-carboxyaminoimidazole ribonucleotide mutase from Staphylococcus aureus

Brugarolas, P.; Duguid, E.M.; Zhang, W.; Poor, C.B.; He, C.; Acta Crystallogr. Sect. D 67, 707-715 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene purE, expression of His-tagged enzyme in Escherichia coli strain BL21 Star (DE3)
Staphylococcus aureus
Crystallization (Commentary)
Crystallization
Organism
purified recombinant detagged enzyme, crystallization at room temperature, 10 mg/ml protein is mixed with a reservoir solution consisting of 0.1 M sodium acetate trihydrate, pH 4.5, and 2 M ammonium sulfate, 24 h, X-ray diffraction structure determination and analysis at 1.45 Aresolution, molecular replacement using the structure of Bacillus anthracis PurE, PDB ID 1xmp, as template
Staphylococcus aureus
Engineering
Amino acid exchange
Commentary
Organism
H38F
site-directed mutagenesis of the catalytic residue renders the enzyme inactive
Staphylococcus aureus
H38N
site-directed mutagenesis of the catalytic residue renders the enzyme inactive
Staphylococcus aureus
H38W
site-directed mutagenesis of the catalytic residue renders the enzyme inactive
Staphylococcus aureus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Staphylococcus aureus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
Staphylococcus aureus
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Staphylococcus aureus
A6QFS3
gene purE
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography, tag cleavage by TEV protease, and gel filtration
Staphylococcus aureus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
726578
Staphylococcus aureus
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
-
-
?
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Staphylococcus aureus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
assay at
Staphylococcus aureus
Cloned(Commentary) (protein specific)
Commentary
Organism
gene purE, expression of His-tagged enzyme in Escherichia coli strain BL21 Star (DE3)
Staphylococcus aureus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant detagged enzyme, crystallization at room temperature, 10 mg/ml protein is mixed with a reservoir solution consisting of 0.1 M sodium acetate trihydrate, pH 4.5, and 2 M ammonium sulfate, 24 h, X-ray diffraction structure determination and analysis at 1.45 Aresolution, molecular replacement using the structure of Bacillus anthracis PurE, PDB ID 1xmp, as template
Staphylococcus aureus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
H38F
site-directed mutagenesis of the catalytic residue renders the enzyme inactive
Staphylococcus aureus
H38N
site-directed mutagenesis of the catalytic residue renders the enzyme inactive
Staphylococcus aureus
H38W
site-directed mutagenesis of the catalytic residue renders the enzyme inactive
Staphylococcus aureus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
required
Staphylococcus aureus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
Staphylococcus aureus
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography, tag cleavage by TEV protease, and gel filtration
Staphylococcus aureus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
726578
Staphylococcus aureus
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
-
-
?
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Staphylococcus aureus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.8
-
assay at
Staphylococcus aureus
General Information
General Information
Commentary
Organism
additional information
His38 is essential for function, role of His38 as a general acid/base catalyst, structure analysis, comparison to Homo sapiens class II PurE enzyme, active site structure, overview
Staphylococcus aureus
General Information (protein specific)
General Information
Commentary
Organism
additional information
His38 is essential for function, role of His38 as a general acid/base catalyst, structure analysis, comparison to Homo sapiens class II PurE enzyme, active site structure, overview
Staphylococcus aureus
Other publictions for EC 5.4.99.18
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)
747257
Lei
Identification of B. anthraci ...
Bacillus anthracis
Bioorg. Med. Chem.
24
596-605
2016
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1
1
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-
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16
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1
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3
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1
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16
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1
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1
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1
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2
2
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747253
Kim
Identification of Bacillus an ...
Bacillus anthracis
Bioorg. Med. Chem.
23
1492-1499
2015
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1
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6
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1
1
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6
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1
1
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1
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726578
Brugarolas
Structural and biochemical cha ...
Staphylococcus aureus
Acta Crystallogr. Sect. D
67
707-715
2011
-
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1
1
3
-
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1
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1
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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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678260
Hoskins
N5-CAIR mutase: role of a CO2 ...
Escherichia coli
Biochemistry
46
2842-2855
2007
-
-
1
1
3
-
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1
-
-
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2
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1
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2
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5
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3
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2
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5
-
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678322
Schaefer
Multiple active site histidine ...
Acetobacter aceti
Biochemistry
46
9507-9512
2007
-
-
-
1
-
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-
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3
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678203
Constantine
Biochemical and structural stu ...
Acetobacter aceti
Biochemistry
45
8193-8208
2006
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-
1
1
11
-
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7
-
-
4
-
-
4
-
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1
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1
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2
1
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1
8
-
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1
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1
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1
11
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7
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4
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1
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2
1
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1
8
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1
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660590
Settembre
Acidophilic adaptations in the ...
Acetobacter aceti
Acta Crystallogr. Sect. D
60
1753-1760
2004
-
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1
-
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4
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663353
Schwarzenbacher
Crystal structure of a phospho ...
Thermotoga maritima
Proteins
55
474-478
2004
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1
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1
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649890
Meyer
Evidence for the Direct Transf ...
Escherichia coli
Biochemistry
38
3012-3018
1999
-
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3
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1
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663416
Mathews
Crystal structure of Escherich ...
Escherichia coli
Structure
7
1395-1406
1999
-
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1
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661777
Sorensen
Identification and sequence an ...
Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617
FEMS Microbiol. Lett.
154
173-180
1997
-
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1
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5
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661776
Chung
Genomic organization of purK a ...
Corynebacterium ammoniagenes
FEMS Microbiol. Lett.
137
265-268
1996
-
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1
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661050
Mueller
N5-carboxyaminoimidazole ribon ...
Escherichia coli
Biochemistry
33
2269-2278
1994
-
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1268
Meyer
Purification and characterizat ...
Escherichia coli
Biochemistry
31
5022-5032
1992
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661977
Watanabe
Identification and sequence an ...
Escherichia coli, Escherichia coli NK6051
J. Bacteriol.
171
198-204
1989
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