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show all sequences of 1.13.11.48

Stability, unfolding, and structural changes of cofactor-free 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase

Beermann, B; Guddorf, J.; Boehm,‡ K.; Albers, A.; Kolkenbrock, S.; Fetzner, S.; Hinz, H.-J.; Biochemistry 46, 4241-4249 (2007)

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
an oxidatively stable mutant variant
Paenarthrobacter nitroguajacolicus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Paenarthrobacter nitroguajacolicus
-
-
-
Paenarthrobacter nitroguajacolicus Rü61a
-
-
-
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
Subunits
Subunits
Commentary
Organism
More
at 25°C, recombinant His6-tagged HodC has a hydrodynamic radius of 2.3 nm and an unusually high degree of alpha-helical structure of about 60%, based on deconvolution of CD spectra. The percentage of beta-sheets and -turns is expected to be relatively low in view of its sequence similarity to proteins of the alpha/beta-hydrolase fold superfamily, transition two-state model, overview
Paenarthrobacter nitroguajacolicus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
recombinant His6HodC exhibits three-state unfolding with an intermediate state I that exhibits at the transition temperature a volume larger than that of the native or denatured state. The intermediate state I is also associated with the highest isothermal expansion coefficient, alphaP, of the three states and exhibits a significantly lower percentage of R-helical structure than the native state. The stability difference between the native and intermediate state is rather small which makes I a potential candidate for reactions with various ligands, particularly those having a preference for the apparently preserved beta-type motifs
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
an oxidatively stable mutant variant
Paenarthrobacter nitroguajacolicus
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
Subunits (protein specific)
Subunits
Commentary
Organism
More
at 25°C, recombinant His6-tagged HodC has a hydrodynamic radius of 2.3 nm and an unusually high degree of alpha-helical structure of about 60%, based on deconvolution of CD spectra. The percentage of beta-sheets and -turns is expected to be relatively low in view of its sequence similarity to proteins of the alpha/beta-hydrolase fold superfamily, transition two-state model, overview
Paenarthrobacter nitroguajacolicus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
additional information
-
recombinant His6HodC exhibits three-state unfolding with an intermediate state I that exhibits at the transition temperature a volume larger than that of the native or denatured state. The intermediate state I is also associated with the highest isothermal expansion coefficient, alphaP, of the three states and exhibits a significantly lower percentage of R-helical structure than the native state. The stability difference between the native and intermediate state is rather small which makes I a potential candidate for reactions with various ligands, particularly those having a preference for the apparently preserved beta-type motifs
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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4
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1
1
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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
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1
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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
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1
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3
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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
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1
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17
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18
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12
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1
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20
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17
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18
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12
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20
1
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1
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658042
Frerichs-Deeken
Dioxygenases without requireme ...
Paenarthrobacter ilicis, Paenarthrobacter ilicis Ru61a
Biochemistry
43
14485-14499
2004
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4
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2
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285259
Fischer
Bacterial 2,4-dioxygenases: ne ...
Arthrobacter sp.
J. Bacteriol.
181
5725-5733
1999
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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
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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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