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Literature summary for 1.13.11.48 extracted from

  • Boehm, K.; Guddorf, J.; Albers, A.; Kamiyama, T.; Fetzner, S.; Hinz, H.
    Thermodynamic analysis of denaturant-induced unfolding of HodC69S protein supports a three-state mechanism (2008), Biochemistry, 47, 7116-7126.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant N-terminally His6-tagged HODs in Escherichia coli strain M15 Paenarthrobacter nitroguajacolicus

Protein Variants

Protein Variants Comment Organism
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
C69S site-directed mutagenesis, thermodynamic analysis of denaturant-induced unfolding of the mutant compared to the wild-type enzyme, overview Paenarthrobacter nitroguajacolicus

Inhibitors

Inhibitors Comment 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 Comment 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] Comment Organism
33240
-
calculated Paenarthrobacter nitroguajacolicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment Textmining
Paenarthrobacter nitroguajacolicus
-
-
-
Paenarthrobacter nitroguajacolicus Q7WSQ7
-
-
Paenarthrobacter nitroguajacolicus R-61a
-
-
-
Paenarthrobacter nitroguajacolicus Rü61a Q7WSQ7
-
-

Purification (Commentary)

Purification (Comment) 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] Comment Organism
70
-
sodium phosphate buffer, 30°C, pH 7.5 Paenarthrobacter nitroguajacolicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1H-3-Hydroxy-4-oxoquinaldine + O2
-
Paenarthrobacter nitroguajacolicus N-Acetylanthranilate + CO
-
?
1H-3-Hydroxy-4-oxoquinaldine + O2
-
Paenarthrobacter nitroguajacolicus Rü61a N-Acetylanthranilate + CO
-
?
1H-3-hydroxy-4-oxoquinaldine + O2 cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation Paenarthrobacter nitroguajacolicus ?
-
?
1H-3-hydroxy-4-oxoquinaldine + O2 cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation Paenarthrobacter nitroguajacolicus R-61a ?
-
?

Subunits

Subunits Comment Organism
monomer 1 * 33240 Paenarthrobacter nitroguajacolicus

Synonyms

Synonyms Comment Organism
1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
-
Paenarthrobacter nitroguajacolicus
HOD
-
Paenarthrobacter nitroguajacolicus
More HOD belongs to the alpha/beta-hydrolase-fold superfamily of enzymes Paenarthrobacter nitroguajacolicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Paenarthrobacter nitroguajacolicus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment 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 Comment Organism
additional information thermodynamic analysis of denaturant-induced unfolding of Hod C69Smutant protein supports a three-state mechanism Paenarthrobacter nitroguajacolicus