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 (Comment) | Organism |
---|---|
expression of recombinant N-terminally Strep-tagged enzyme in Escherichia coli strain BL21(DE3) | Trigonopsis variabilis |
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 | 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Trigonopsis variabilis | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant N-terminally Strep-tagged enzyme to homogeneity from Escherichia coli strain BL21(DE3) by affinity chromatography | Trigonopsis variabilis |
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 | Comment | Organism |
---|---|---|
DAO | - |
Trigonopsis variabilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Trigonopsis variabilis |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Trigonopsis variabilis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Trigonopsis variabilis |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme is involved in the conversion of cephalosporin C | Trigonopsis variabilis |