Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.5.99.15 extracted from

  • Garg, A.; Sinha, S.
    Factors deciding the assembly and thermostability of the DmrB cage (2021), Int. J. Biol. Macromol., 182, 959-967 .
    View publication on PubMed
Search for more literature for 1.5.99.15

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Paraburkholderia xenovorans

Organism

Organism UniProt Comment Textmining
Paraburkholderia xenovorans Q13QT8
-
-

Renatured (Commentary)

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

Subunits Comment Organism
multimer enzyme has a didodecamer (24mer) structure consisting of 8 trimeric subunits, cysallization data Paraburkholderia xenovorans

Synonyms

Synonyms Comment Organism
Bxe_B2440
-
 Paraburkholderia xenovorans
DmrB
-
 Paraburkholderia xenovorans

Temperature Stability [°C]

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

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