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Literature summary 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.13.11.48 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
1.13.11.48 C69S site-directed mutagenesis, thermodynamic analysis of denaturant-induced unfolding of the mutant compared to the wild-type enzyme, overview Paenarthrobacter nitroguajacolicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.11.48 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
1.13.11.48 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.13.11.48 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.11.48 33240
-
 calculated Paenarthrobacter nitroguajacolicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.13.11.48 1H-3-Hydroxy-4-oxoquinaldine + O2 Paenarthrobacter nitroguajacolicus
-
 N-Acetylanthranilate + CO
-
 ?
1.13.11.48 1H-3-hydroxy-4-oxoquinaldine + O2 Paenarthrobacter nitroguajacolicus cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation ?
-
 ?
1.13.11.48 1H-3-Hydroxy-4-oxoquinaldine + O2 Paenarthrobacter nitroguajacolicus Rü61a
-
 N-Acetylanthranilate + CO
-
 ?
1.13.11.48 1H-3-hydroxy-4-oxoquinaldine + O2 Paenarthrobacter nitroguajacolicus R-61a cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.13.11.48 Paenarthrobacter nitroguajacolicus
-
-
-
1.13.11.48 Paenarthrobacter nitroguajacolicus Q7WSQ7
-
-
1.13.11.48 Paenarthrobacter nitroguajacolicus R-61a
-
-
-
1.13.11.48 Paenarthrobacter nitroguajacolicus Rü61a Q7WSQ7
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.11.48 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]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.13.11.48 70
-
 sodium phosphate buffer, 30°C, pH 7.5 Paenarthrobacter nitroguajacolicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.11.48 1H-3-Hydroxy-4-oxoquinaldine + O2
-
 Paenarthrobacter nitroguajacolicus N-Acetylanthranilate + CO
-
 ?
1.13.11.48 1H-3-Hydroxy-4-oxoquinaldine + O2
-
 Paenarthrobacter nitroguajacolicus Rü61a N-Acetylanthranilate + CO
-
 ?
1.13.11.48 1H-3-hydroxy-4-oxoquinaldine + O2 cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation Paenarthrobacter nitroguajacolicus ?
-
 ?
1.13.11.48 1H-3-hydroxy-4-oxoquinaldine + O2 cleavage of substrate, involved in quinalidine (2-methylquinoline) degradation Paenarthrobacter nitroguajacolicus R-61a ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.13.11.48 monomer 1 * 33240 Paenarthrobacter nitroguajacolicus

Synonyms

EC Number Synonyms Comment Organism
1.13.11.48 1H-3-Hydroxy-4-oxoquinaldine 2,4-dioxygenase
-
 Paenarthrobacter nitroguajacolicus
1.13.11.48 HOD
-
 Paenarthrobacter nitroguajacolicus
1.13.11.48 More HOD belongs to the alpha/beta-hydrolase-fold superfamily of enzymes Paenarthrobacter nitroguajacolicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.11.48 30
-
 assay at Paenarthrobacter nitroguajacolicus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.13.11.48 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
1.13.11.48 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

EC Number General Information Comment Organism
1.13.11.48 additional information thermodynamic analysis of denaturant-induced unfolding of Hod C69Smutant protein supports a three-state mechanism Paenarthrobacter nitroguajacolicus