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Literature summary for 1.1.3.10 extracted from

  • Maresova, H.; Palyzova, A.; Kyslik, P.
    The C-terminal region controls correct folding of genus Trametes pyranose 2-oxidases (2007), J. Biotechnol., 130, 229-235.
    View publication on PubMed
Search for more literature for 1.1.3.10

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21-DE3, recombinant host strains shown to be different in formation of inclusion bodies at higher growth temperatures, plasmids pSE33 and pRQ5 used for site-directed recombination Trametes pubescens
expressed in Escherichia coli BL21-DE3, recombinant host strains shown to be different in formation of inclusion bodies between inserts of Trametes ochracea and Trametes pubescens at higher growth temperatures, plasmids pSE33 and pRQ5 used for site-directed recombination Trametes ochracea

Organism

Organism UniProt Comment Textmining
Trametes ochracea Q7ZA32
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-
Trametes pubescens Q5G234
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant protein, gel purification and SDS-PAGE Trametes ochracea
recombinant protein, gel purification and SDS-PAGE Trametes pubescens

Source Tissue

Source Tissue Comment Organism Textmining
culture supernatant
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 Trametes ochracea
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culture supernatant
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 Trametes pubescens
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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 comparative characterization of pyranose 2-oxidase from Trametes ochracea and Trametes pubescens, 93.4% identity of amino acid sequences observed, specific activity of pyranose 2-oxidase from Trametes pubescens eight times higher than that from Trametes ochracea, pyranose 2-oxidase ctivity determined in a peroxidase-coupled assay, site-directed recombination performed, pyranose 2-oxidases of Trametes pubescens shown to exhibit a unique trait regarding protein folding at growth temperature of 28°C Trametes pubescens
additional information
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 comparative characterization of pyranose 2-oxidase from Trametes ochracea and Trametes pubescens, enzyme activity determined by the formation of H2O2 in a peroxidase-coupled assay, inclusion body formation and specific activity of pyranose 2-oxidases in Escherichia coli harbouring chimeric plasmid constructs, site-directed recombination Trametes ochracea

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + O2 recombinant pyranose 2-oxidase analyzed Trametes ochracea 2-dehydro-D-glucose + H2O2
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 ?
D-glucose + O2 recombinant pyranose 2-oxidase analyzed Trametes pubescens 2-dehydro-D-glucose + H2O2
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 ?