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show all sequences of 1.13.11.48

Thermodynamic analysis of denaturant-induced unfolding of HodC69S protein supports a three-state mechanism

Boehm, K.; Guddorf, J.; Albers, A.; Kamiyama, T.; Fetzner, S.; Hinz, H.; Biochemistry 47, 7116-7126 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression of wild-type and mutant N-terminally His6-tagged HODs in Escherichia coli strain M15
Paenarthrobacter nitroguajacolicus
Engineering
Amino acid exchange
Commentary
Organism
C69S
catalytical properties unchanged, mutant enzyme with hexahistidine tag at N-terminus and amino acid exchange influencing disulfide binding between C37 and C184; site-directed mutagenesis, thermodynamic analysis of denaturant-induced unfolding of the mutant compared to the wild-type enzyme, overview
Paenarthrobacter nitroguajacolicus
Inhibitors
Inhibitors
Commentary
Organism
Structure
guanidine hydrochloride
almost linear decrease of activity up to 1 M where activity vanishes, three-state unfolding of mutant enzyme; causes isothermal unfolding of mutant C69S in a three-state mechanism, thermodynamic analysis, overview
Paenarthrobacter nitroguajacolicus
Urea
causes isothermal unfolding of mutant C69S in a three-state mechanism, thermodynamic analysis, overview; nonlinear decrease of activity, activity lost at about 5 M, three-state unfolding of mutant enzyme
Paenarthrobacter nitroguajacolicus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
comparison of thermodynamic parameters for GdnHCl- and urea-induced unfolding of His6HodC69S in 10 mM sodium phosphate and 10 mM sodium borate, pH 7.5, at 25°C, overview
Paenarthrobacter nitroguajacolicus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33240
-
calculated
Paenarthrobacter nitroguajacolicus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1H-3-Hydroxy-4-oxoquinaldine + O2
Paenarthrobacter nitroguajacolicus
-
N-Acetylanthranilate + CO
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
Paenarthrobacter nitroguajacolicus
cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
?
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
Paenarthrobacter nitroguajacolicus Rü61a
-
N-Acetylanthranilate + CO
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
Paenarthrobacter nitroguajacolicus R-61a
cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
?
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Paenarthrobacter nitroguajacolicus
-
-
-
Paenarthrobacter nitroguajacolicus
Q7WSQ7
-
-
Paenarthrobacter nitroguajacolicus R-61a
-
-
-
Paenarthrobacter nitroguajacolicus Rü61a
Q7WSQ7
-
-
Purification (Commentary)
Commentary
Organism
recombinant wild-type and mutant N-terminally His6-tagged HODs from Escherichia coli strain M15 by nickel affinity and anion exchange chromatography
Paenarthrobacter nitroguajacolicus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
70
-
sodium phosphate buffer, 30°C, pH 7.5
Paenarthrobacter nitroguajacolicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1H-3-Hydroxy-4-oxoquinaldine + O2
-
696277
Paenarthrobacter nitroguajacolicus
N-Acetylanthranilate + CO
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
-
696277
Paenarthrobacter nitroguajacolicus Rü61a
N-Acetylanthranilate + CO
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
696277
Paenarthrobacter nitroguajacolicus
?
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
696277
Paenarthrobacter nitroguajacolicus R-61a
?
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 33240
Paenarthrobacter nitroguajacolicus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Paenarthrobacter nitroguajacolicus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
10
40
enzyme in native reduced state (40 mM dithiothreitol) of mutant enzyme, 10 mM sodium phosphate and 10 mM sodium borate buffer, pH 7.5, unfolding starts at 40°C
Paenarthrobacter nitroguajacolicus
10
50
native oxidized state of mutant enzyme, 10 mM sodium phosphate and 10 mM sodium borate buffer, pH 7.5, unfolding starts at 50°C
Paenarthrobacter nitroguajacolicus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression of wild-type and mutant N-terminally His6-tagged HODs in Escherichia coli strain M15
Paenarthrobacter nitroguajacolicus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C69S
site-directed mutagenesis, thermodynamic analysis of denaturant-induced unfolding of the mutant compared to the wild-type enzyme, overview
Paenarthrobacter nitroguajacolicus
C69S
catalytical properties unchanged, mutant enzyme with hexahistidine tag at N-terminus and amino acid exchange influencing disulfide binding between C37 and C184
Paenarthrobacter nitroguajacolicus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
guanidine hydrochloride
causes isothermal unfolding of mutant C69S in a three-state mechanism, thermodynamic analysis, overview
Paenarthrobacter nitroguajacolicus
guanidine hydrochloride
almost linear decrease of activity up to 1 M where activity vanishes, three-state unfolding of mutant enzyme
Paenarthrobacter nitroguajacolicus
Urea
causes isothermal unfolding of mutant C69S in a three-state mechanism, thermodynamic analysis, overview
Paenarthrobacter nitroguajacolicus
Urea
nonlinear decrease of activity, activity lost at about 5 M, three-state unfolding of mutant enzyme
Paenarthrobacter nitroguajacolicus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
comparison of thermodynamic parameters for GdnHCl- and urea-induced unfolding of His6HodC69S in 10 mM sodium phosphate and 10 mM sodium borate, pH 7.5, at 25°C, overview
Paenarthrobacter nitroguajacolicus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33240
-
calculated
Paenarthrobacter nitroguajacolicus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
1H-3-Hydroxy-4-oxoquinaldine + O2
Paenarthrobacter nitroguajacolicus
-
N-Acetylanthranilate + CO
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
Paenarthrobacter nitroguajacolicus
cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
?
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
Paenarthrobacter nitroguajacolicus Rü61a
-
N-Acetylanthranilate + CO
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
Paenarthrobacter nitroguajacolicus R-61a
cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
?
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type and mutant N-terminally His6-tagged HODs from Escherichia coli strain M15 by nickel affinity and anion exchange chromatography
Paenarthrobacter nitroguajacolicus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
70
-
sodium phosphate buffer, 30°C, pH 7.5
Paenarthrobacter nitroguajacolicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1H-3-Hydroxy-4-oxoquinaldine + O2
-
696277
Paenarthrobacter nitroguajacolicus
N-Acetylanthranilate + CO
-
-
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
-
696277
Paenarthrobacter nitroguajacolicus Rü61a
N-Acetylanthranilate + CO
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
696277
Paenarthrobacter nitroguajacolicus
?
-
-
-
?
1H-3-hydroxy-4-oxoquinaldine + O2
cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation
696277
Paenarthrobacter nitroguajacolicus R-61a
?
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 33240
Paenarthrobacter nitroguajacolicus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Paenarthrobacter nitroguajacolicus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
10
40
enzyme in native reduced state (40 mM dithiothreitol) of mutant enzyme, 10 mM sodium phosphate and 10 mM sodium borate buffer, pH 7.5, unfolding starts at 40°C
Paenarthrobacter nitroguajacolicus
10
50
native oxidized state of mutant enzyme, 10 mM sodium phosphate and 10 mM sodium borate buffer, pH 7.5, unfolding starts at 50°C
Paenarthrobacter nitroguajacolicus
General Information
General Information
Commentary
Organism
additional information
thermodynamic analysis of denaturant-induced unfolding of Hod C69Smutant protein supports a three-state mechanism
Paenarthrobacter nitroguajacolicus
General Information (protein specific)
General Information
Commentary
Organism
additional information
thermodynamic analysis of denaturant-induced unfolding of Hod C69Smutant protein supports a three-state mechanism
Paenarthrobacter nitroguajacolicus
Other publictions for EC 1.13.11.48
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)
742251
Pietra
Binding pockets and permeatio ...
Paenarthrobacter nitroguajacolicus
Chem. Biodivers.
11
861-871
2014
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696277
Boehm
Thermodynamic analysis of dena ...
Paenarthrobacter nitroguajacolicus, Paenarthrobacter nitroguajacolicus R-61a, Paenarthrobacter nitroguajacolicus Rü61a
Biochemistry
47
7116-7126
2008
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1
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1
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2
1
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1
4
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5
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1
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4
1
1
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2
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1
1
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684175
Steiner
Crystallization and preliminar ...
Paenarthrobacter nitroguajacolicus, Paenarthrobacter nitroguajacolicus Rü61a, Paenarthrobacter nitroguajacolicus Rue61a
Acta Crystallogr. Sect. F
63
382-385
2007
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1
1
2
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4
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1
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1
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1
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1
2
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3
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1
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3
1
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-
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714163
Beermann
Stability, unfolding, and stru ...
Paenarthrobacter nitroguajacolicus, Paenarthrobacter nitroguajacolicus Rü61a
Biochemistry
46
4241-4249
2007
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-
1
-
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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1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
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673207
Frerichs-Deeken
Dioxygenases without requireme ...
Paenarthrobacter nitroguajacolicus, Paenarthrobacter nitroguajacolicus R-61a, Paenarthrobacter nitroguajacolicus Rü61a
Curr. Microbiol.
51
344-352
2005
-
-
1
-
17
-
-
18
-
-
-
3
-
4
-
-
1
1
-
-
-
-
12
-
1
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20
1
2
1
-
-
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1
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-
17
-
-
-
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18
-
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3
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1
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-
12
-
1
-
-
20
1
2
1
-
-
-
-
-
-
-
658042
Frerichs-Deeken
Dioxygenases without requireme ...
Paenarthrobacter ilicis, Paenarthrobacter ilicis Ru61a
Biochemistry
43
14485-14499
2004
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-
1
-
1
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2
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2
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4
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2
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1
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1
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2
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4
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2
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-
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-
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-
285259
Fischer
Bacterial 2,4-dioxygenases: ne ...
Arthrobacter sp.
J. Bacteriol.
181
5725-5733
1999
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1
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2
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207895
Bauer
2,4-Dioxygenases catalyzing N- ...
Arthrobacter sp., Arthrobacter sp. Ru61a
Eur. J. Biochem.
240
576-583
1996
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8
1
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1
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3
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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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1
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8
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1
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1
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1
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4
1
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207896
Bauer
-
A novel type of oxygenolytic r ...
Arthrobacter sp., Arthrobacter sp. Ru61a
FEMS Microbiol. Lett.
117
299-304
1994
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