Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Paraburkholderia xenovorans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Paraburkholderia xenovorans | Q13QT8 | - |
- |
Renatured (Comment) | Organism |
---|---|
enzyme displays a concentration-dependant self-assembly which is mediated by ionic interactions. The cofactor FMN stabilizes and preserves the secondary and quaternary structure of DmrB against thermal insult | Paraburkholderia xenovorans |
Subunits | Comment | Organism |
---|---|---|
multimer | enzyme has a didodecamer (24mer) structure consisting of 8 trimeric subunits, cysallization data | Paraburkholderia xenovorans |
Synonyms | Comment | Organism |
---|---|---|
Bxe_B2440 | - |
Paraburkholderia xenovorans |
DmrB | - |
Paraburkholderia xenovorans |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
55 | - |
apo-form of DmrB retains the secondary structure till 55°C | Paraburkholderia xenovorans |
84 | - |
holo-form of DmrB retains the secondary structure till a temperature of 84°C | Paraburkholderia xenovorans |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FMN | DmrB contains 2 FMN molecules on the active site at the monomer-monomer interface. The FMN-1 molecule shows ionic interactions with residues Ser110 and Asn116 along with some non-bonded contacts. The FMN-2 molecule shows ionic contacts with Lys123 and Gln120 and pi-pi stacking with the Tyr85 residue. FMN stabilizes and preserves the secondary and quaternary structure of DmrB against thermal insult | Paraburkholderia xenovorans |