BRENDA - Enzyme Database show
show all sequences of 5.4.99.18

N5-CAIR mutase: role of a CO2 binding site and substrate movement in catalysis

Hoskins, A.A.; Morar, M.; Kappock, T.J.; Mathews, I.I.; Zaugg, J.B.; Barder, T.E.; Peng, P.; Okamoto, A.; Ealick, S.E.; Stubbe, J.; Biochemistry 46, 2842-2855 (2007)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Escherichia coli
Crystallization (Commentary)
Crystallization
Organism
wild-type cocrystallized with 4-nitroaminoimidazole ribonucleotide and mutants H45N and H45Q soaked with 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
H45N
very low catalytic activity
Escherichia coli
H45Q
very low catalytic activity
Escherichia coli
H45W
very low catalytic activity
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0226
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
wild-type, pH 7.5, 23°C
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P0AG18
-
-
Reaction
Reaction
Commentary
Organism
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
common, buried carboxylate or CO2 binding site for substrate and product in a hydrophobic pocket, in which the carboxylate or CO2 interacts with backbone amides. The carboxylate orients the substrate for proton transfer from His45 to 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole to form an enzyme-bound aminoimidazole ribonucleotide and CO2 intermediate. subsequent movement of the aminoimidazole moiety reorients it for addition of CO2 at C4 to generate iso-5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate. H5 is now in a position to remove a C4 proton to produce 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
678260
Escherichia coli
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
-
-
r
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
678260
Escherichia coli
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
-
-
r
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0004
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H45W, pH 7.5, 23°C
Escherichia coli
0.0012
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H45Q, pH 7.5, 23°C
Escherichia coli
0.0021
-
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
mutant H45Q, pH 7.5, 23°C
Escherichia coli
15.5
-
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
wild-type, pH 7.5, 23°C
Escherichia coli
15.6
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
wild-type, pH 7.5, 23°C
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
wild-type cocrystallized with 4-nitroaminoimidazole ribonucleotide and mutants H45N and H45Q soaked with 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
H45N
very low catalytic activity
Escherichia coli
H45Q
very low catalytic activity
Escherichia coli
H45W
very low catalytic activity
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0226
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
wild-type, pH 7.5, 23°C
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
678260
Escherichia coli
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
-
-
r
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
678260
Escherichia coli
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
-
-
r
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0004
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H45W, pH 7.5, 23°C
Escherichia coli
0.0012
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H45Q, pH 7.5, 23°C
Escherichia coli
0.0021
-
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
mutant H45Q, pH 7.5, 23°C
Escherichia coli
15.5
-
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
wild-type, pH 7.5, 23°C
Escherichia coli
15.6
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
wild-type, pH 7.5, 23°C
Escherichia coli
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
-
1
1
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16
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1
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16
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1
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1
-
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
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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
1
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678260
Hoskins
N5-CAIR mutase: role of a CO2 ...
Escherichia coli
Biochemistry
46
2842-2855
2007
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-
1
1
3
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1
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2
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5
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1
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1
3
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1
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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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1
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678203
Constantine
Biochemical and structural stu ...
Acetobacter aceti
Biochemistry
45
8193-8208
2006
-
-
1
1
11
-
-
7
-
-
4
-
-
4
-
-
-
1
-
-
1
-
2
1
-
-
1
8
-
-
1
-
-
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1
-
1
11
-
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7
-
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4
-
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-
1
-
2
1
-
-
1
8
-
-
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
-
-
-
1
-
-
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-
-
-
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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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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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1
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661777
Sorensen
Identification and sequence an ...
Saccharolobus solfataricus, Saccharolobus solfataricus DSM 1617
FEMS Microbiol. Lett.
154
173-180
1997
-
-
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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3
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1
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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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