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Literature summary for 1.13.11.48 extracted from

  • Beermann, B; Guddorf, J.; Boehm,‡ K.; Albers, A.; Kolkenbrock, S.; Fetzner, S.; Hinz, H.-J.
    Stability, unfolding, and structural changes of cofactor-free 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (2007), Biochemistry, 46, 4241-4249.
    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 an oxidatively stable mutant variant Paenarthrobacter nitroguajacolicus

Organism

Organism UniProt Comment Textmining
Paenarthrobacter nitroguajacolicus
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Paenarthrobacter nitroguajacolicus Rü61a
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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

Subunits

Subunits Comment 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

Synonyms

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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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