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Literature summary 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

EC Number Application Comment Organism
1.4.3.3 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.4.3.3 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

EC Number General Stability Organism
1.4.3.3 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)

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

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.3 Trigonopsis variabilis
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.4.3.3 DAO
-
 Trigonopsis variabilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.4.3.3 30
-
 assay at Trigonopsis variabilis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.3.3 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.3 8
-
 assay at Trigonopsis variabilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.3 FAD
-
 Trigonopsis variabilis

General Information

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