BRENDA - Enzyme Database show
show all sequences of 5.4.99.18

Biochemical and structural studies of N5-carboxyaminoimidazole ribonucleotide mutase from the acidophilic bacterium Acetobacter aceti

Constantine, C.Z.; Starks, C.M.; Mill, C.P.; Ransome, A.E.; Karpowicz, S.J.; Francois, J.A.; Goodman, R.A.; Kappock, T.J.; Biochemistry 45, 8193-8208 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
enzyme is active in Escherichia coli
Acetobacter aceti
Crystallization (Commentary)
Crystallization
Organism
mutant H59N soaked in 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, protonation of 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate C4 may occur in absence of H59
Acetobacter aceti
Engineering
Amino acid exchange
Commentary
Organism
H59A
inactive
Acetobacter aceti
H59D
0.16% of wild-type activity
Acetobacter aceti
H59F
inactive
Acetobacter aceti
H59N
inactive, crystallization data
Acetobacter aceti
H59Q
almost inactive
Acetobacter aceti
H59S
inactive
Acetobacter aceti
H89D
4.4% of wild-type activity
Acetobacter aceti
H89F
14% of wild-type activity
Acetobacter aceti
H89G
91% of wild-type activity
Acetobacter aceti
H89N
2.9% of wild-type activity
Acetobacter aceti
H89V
17% of wild-type activity
Acetobacter aceti
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0007
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89G, 37°C, pH 8.0
Acetobacter aceti
0.0014
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89N, 37°C, pH 8.0
Acetobacter aceti
0.006
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89D, 37°C, pH 8.0
Acetobacter aceti
0.008
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89V, 37°C, pH 8.0; wild-type, 37°C, pH 8.0
Acetobacter aceti
0.009
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89F, 37°C, pH 8.0
Acetobacter aceti
0.03
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H59Q, 37°C, pH 8.0
Acetobacter aceti
0.2
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H59D, 37°C, pH 8.0
Acetobacter aceti
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
18864
-
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
Acetobacter aceti
18900
-
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
Acetobacter aceti
21000
-
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
Acetobacter aceti
197000
-
gel filtration
Acetobacter aceti
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Acetobacter aceti
Q2QJL2
-
-
Reaction
Reaction
Commentary
Organism
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
H89 is not essential and does not function as part of a proton relay system. For synthesis of 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, the carboxylate moiety is positioned in a small pocket proposed to facilitate nucleotide decarboxylation. In the reverse direction, enzyme favors protonation of 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate C4
Acetobacter aceti
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
36
-
pH 8.0, 37°C, direction of decarboxylation of 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Acetobacter aceti
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
-
678203
Acetobacter aceti
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
-
-
r
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
678203
Acetobacter aceti
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
-
-
r
Subunits
Subunits
Commentary
Organism
octamer
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
Acetobacter aceti
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
85
-
melting temperature
Acetobacter aceti
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0006
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H59Q, 37°C, pH 8.0
Acetobacter aceti
0.063
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89N, 37°C, pH 8.0
Acetobacter aceti
0.4
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89D, 37°C, pH 8.0
Acetobacter aceti
0.49
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H59D, 37°C, pH 8.0
Acetobacter aceti
0.97
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89G, 37°C, pH 8.0
Acetobacter aceti
1.97
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89F, 37°C, pH 8.0
Acetobacter aceti
2.1
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89V, 37°C, pH 8.0
Acetobacter aceti
12.2
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
wild-type, 37°C, pH 8.0
Acetobacter aceti
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
7
-
maximum of enzyme stability near pH 7.0
Acetobacter aceti
Cloned(Commentary) (protein specific)
Commentary
Organism
enzyme is active in Escherichia coli
Acetobacter aceti
Crystallization (Commentary) (protein specific)
Crystallization
Organism
mutant H59N soaked in 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate, protonation of 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate C4 may occur in absence of H59
Acetobacter aceti
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
H59A
inactive
Acetobacter aceti
H59D
0.16% of wild-type activity
Acetobacter aceti
H59F
inactive
Acetobacter aceti
H59N
inactive, crystallization data
Acetobacter aceti
H59Q
almost inactive
Acetobacter aceti
H59S
inactive
Acetobacter aceti
H89D
4.4% of wild-type activity
Acetobacter aceti
H89F
14% of wild-type activity
Acetobacter aceti
H89G
91% of wild-type activity
Acetobacter aceti
H89N
2.9% of wild-type activity
Acetobacter aceti
H89V
17% of wild-type activity
Acetobacter aceti
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0007
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89G, 37°C, pH 8.0
Acetobacter aceti
0.0014
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89N, 37°C, pH 8.0
Acetobacter aceti
0.006
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89D, 37°C, pH 8.0
Acetobacter aceti
0.008
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89V, 37°C, pH 8.0; wild-type, 37°C, pH 8.0
Acetobacter aceti
0.009
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89F, 37°C, pH 8.0
Acetobacter aceti
0.03
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H59Q, 37°C, pH 8.0
Acetobacter aceti
0.2
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H59D, 37°C, pH 8.0
Acetobacter aceti
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
18864
-
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
Acetobacter aceti
18900
-
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
Acetobacter aceti
21000
-
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
Acetobacter aceti
197000
-
gel filtration
Acetobacter aceti
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
36
-
pH 8.0, 37°C, direction of decarboxylation of 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
Acetobacter aceti
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
-
678203
Acetobacter aceti
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
-
-
r
5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole
-
678203
Acetobacter aceti
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
octamer
8 * 18900, calculated, 8 * 21000, SDS-PAGE, 8 * 18864, ESI-MS
Acetobacter aceti
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
85
-
melting temperature
Acetobacter aceti
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.0006
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H59Q, 37°C, pH 8.0
Acetobacter aceti
0.063
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89N, 37°C, pH 8.0
Acetobacter aceti
0.4
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89D, 37°C, pH 8.0
Acetobacter aceti
0.49
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H59D, 37°C, pH 8.0
Acetobacter aceti
0.97
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89G, 37°C, pH 8.0
Acetobacter aceti
1.97
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89F, 37°C, pH 8.0
Acetobacter aceti
2.1
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
mutant H89V, 37°C, pH 8.0
Acetobacter aceti
12.2
-
5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate
wild-type, 37°C, pH 8.0
Acetobacter aceti
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
7
-
maximum of enzyme stability near pH 7.0
Acetobacter aceti
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
-
-
-
16
-
-
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1
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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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16
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1
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1
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-
-
1
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
747253
Kim
Identification of Bacillus an ...
Bacillus anthracis
Bioorg. Med. Chem.
23
1492-1499
2015
-
-
1
-
-
-
6
-
-
-
1
1
-
1
-
-
1
-
-
-
-
-
1
1
1
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-
1
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1
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6
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1
1
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1
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1
1
1
-
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-
1
-
-
-
-
-
-
-
-
-
726578
Brugarolas
Structural and biochemical cha ...
Staphylococcus aureus
Acta Crystallogr. Sect. D
67
707-715
2011
-
-
1
1
3
-
-
-
-
1
-
1
-
1
-
-
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
3
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1
-
1
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1
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-
1
-
1
-
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-
1
-
-
-
-
1
1
-
-
-
678260
Hoskins
N5-CAIR mutase: role of a CO2 ...
Escherichia coli
Biochemistry
46
2842-2855
2007
-
-
1
1
3
-
-
1
-
-
-
-
-
2
-
-
-
1
-
-
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2
-
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5
-
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1
-
1
3
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1
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2
-
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-
5
-
-
-
-
-
-
-
-
-
-
678322
Schaefer
Multiple active site histidine ...
Acetobacter aceti
Biochemistry
46
9507-9512
2007
-
-
-
1
-
-
-
-
-
-
-
-
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3
-
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678203
Constantine
Biochemical and structural stu ...
Acetobacter aceti
Biochemistry
45
8193-8208
2006
-
-
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
-
1
11
-
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7
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4
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1
-
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
-
-
-
1
-
-
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4
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1
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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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1
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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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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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