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Literature summary for 1.11.1.13 extracted from

  • Ninomiya, R.; Zhu, B.; Kojima, T.; Iwasaki, Y.; Nakano, H.
    Role of disulfide bond isomerase DsbC, calcium ions, and hemin in cell-free protein synthesis of active manganese peroxidase isolated from Phanerochaete chrysosporium (2014), J. Biosci. Bioeng., 117, 652-657 .
    View publication on PubMed

Application

Application Comment Organism
synthesis expression of active manganese peroxidase in an Escherichia coli cell-free protein synthesis system, and optimization of reaction conditions such as the concentrations of hemin, calcium ions, and disulfide bond isomerase. Cell-free synthesized manganese peroxidase purified using the hemagglutinin tag shows higher specific activity than the commercial wild-type enzyme Phanerodontia chrysosporium

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Phanerodontia chrysosporium

Organism

Organism UniProt Comment Textmining
Phanerodontia chrysosporium
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
17.2
-
recombinant protein, pH 4.5, 37°C Phanerodontia chrysosporium

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Amplex Red + H2O2
-
Phanerodontia chrysosporium ?
-
?