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Literature summary for 1.4.3.3 extracted from
- Contribution of the dimeric state to the thermal stability of the flavoprotein D-amino acid oxidase (2003), Protein Sci., 12, 1018-1029.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | DELTAloop mutant in which 14 residues belonging to a loop connecting strands betaF5-beta-F6 have been deleted is monomeric and thermodynamically less stable than dimeric wild-type DAAO, with melting temperatures of 48°C and 54°C, respectively | Rhodotorula toruloides |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rhodotorula toruloides | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| wild-type enzyme and DELTAloop mutant | Rhodotorula toruloides |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | - |
Rhodotorula toruloides |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DAAO | - |
Rhodotorula toruloides |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 48 | - |
melting temperature of dimeric wild-type enzyme | Rhodotorula toruloides |
| 54 | - |
melting temperature of DELTAloop mutant in which 14 residues belonging to a loop connecting strands betaF5-beta-F6 have been deleted | Rhodotorula toruloides |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | FAD molecule is tightly bound to each 40000 Da subunit | Rhodotorula toruloides |  |
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Release 2023.1 (January 2023)
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