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Literature summary for 1.4.3.3 extracted from

  • Dib, I.; Nidetzky, B.
    The stabilizing effects of immobilization in D-amino acid oxidase from Trigonopsis variabilis (2008), BMC Biotechnol., 8, 72.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
synthesis immobilization of Trigonopsis variabilis D-amino acid oxidase on solid support is the key to a reasonably stable performance of this enzyme in the industrial process for the conversion of cephalosporin C as well as in other biocatalytic applications Trigonopsis variabilis

Cloned(Commentary)

Cloned (Comment) Organism
expression of recombinant N-terminally Strep-tagged enzyme in Escherichia coli strain BL21(DE3) Trigonopsis variabilis

Protein Variants

Protein Variants Comment Organism
additional information immobilization of the recombinant enzyme on solid beads through affinity of its N-terminal Strep-tag to Strep-Tactin coated on insoluble particles, covalent attachment, re-usable in multiple cycles of substrate conversion, the surfactant Pluronic F-68 stabilizes DAO by protecting the enzyme from the deleterious effect of gas-liquid interfaces Trigonopsis variabilis

General Stability

General Stability Organism
the surfactant Pluronic F-68 stabilizes immobilized DAO by protecting the enzyme from the deleterious effect of gas-liquid interfaces Trigonopsis variabilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Trigonopsis variabilis the enzyme is involved in the conversion of cephalosporin C ?
-
?

Organism

Organism UniProt Comment Textmining
Trigonopsis variabilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally Strep-tagged enzyme to homogeneity from Escherichia coli strain BL21(DE3) by affinity chromatography Trigonopsis variabilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-methionine + H2O + 2,6-dichloroindophenol
-
Trigonopsis variabilis ?
-
?
additional information the enzyme is involved in the conversion of cephalosporin C Trigonopsis variabilis ?
-
?

Synonyms

Synonyms Comment Organism
DAO
-
Trigonopsis variabilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Trigonopsis variabilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
inactivation of the enzyme at 50°C proceeds via two main pathways: partial loss of protein structure leading to a denatured holoenzyme, and reversible release of FAD cofactor generating inactive apoenzyme, mechanism, overview Trigonopsis variabilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Trigonopsis variabilis

Cofactor

Cofactor Comment Organism Structure
FAD
-
Trigonopsis variabilis

General Information

General Information Comment Organism
physiological function the enzyme is involved in the conversion of cephalosporin C Trigonopsis variabilis