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

BRENDA support

1.3.3.5: bilirubin oxidase

This is an abbreviated version!
For detailed information about bilirubin oxidase, go to the full flat file.

Word Map on EC 1.3.3.5

Reaction

2 bilirubin +

O2
= 2 biliverdin + 2 H2O

Synonyms

bilirubin oxidase, bilirubin oxidase M-1, bilirubin:oxygen oxidoreductase, blue Cu enzyme, BOD, BODx, BOX, BPUM_0542, copper oxidase, CotA, MCO, multicopper oxidase, MvBO, MvBOD, oxidase, bilirubin

ECTree

     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.3 With oxygen as acceptor
                1.3.3.5 bilirubin oxidase

Cloned

Cloned on EC 1.3.3.5 - bilirubin oxidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Escherichia coli JM109 transformed with pUC119 carrying the CotA gene, produces large amounts of the soluble protein under low-temperature conditions
-
expressed in Aspergillus oryzae
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Origami B (DE3) cells
expressed in Pichia pastoris
-
expressed in Pichia pastoris and Aspergillus oryzae
-
expression in Aspergillus oryzae
-
expression in Aspergillus oryzae, enzyme is in a resting form different from that of authentic bilirubin oxidase, but reaches the resting form of the authentic enzyme after one cycle of reduction and reoxidation with dioxygen
-
expression in Pichia pastoris. The cDNA encoding bilirubin oxidase is cloned into the Pichia pastoris expression vector pPIC9K under the control of the alcohol oxidase 1 promoter and its protein product is secreted using the Saccharomyces alpha-mating factor signal sequence
-
expression in Saccharomyces cerevisiae
-
expression of H94V, H134/136V, C457V, C457A and H456/458V mutants in Aspergillus oryzae
-
gene BPUM_0532, recombinant expression of His-tagged enzyme in Escherichia coli strain Origami B (DE3), evaluation and optimization of a complementary method to optimize the copper oxidase, bilirubin oxidase, enzyme expression in Escherichia coli. Usage of Escherichia coli strain Origami B (DE3), known to promote the formation of disulfide bridges in the bacterial cytoplasm, because the enzyme has a disulfide bridge. In a second step, the effect of coexpression of chaperone proteins (DnaK, DnaJ and GrpE usingthe plasmid pKJE7) on the protein production and specific activity is investigated resulting in an increase of the final amount of enzyme by 858% and its catalytic rate constant by 83%, overview. Comparison of expression efficiency in Escherichia coli strain BL21 (DE3) and Origami B (DE3). When all protein chaperones are expressed together with the r-BOD, the amount of enzyme is largely promoted without impairing the specific activity pointing out the synergy between the two systems, as GroES/GroEL has no effect on the expression alone. Synergy between DnaK, DnaJ, and GrpE, which prevent aggregation of misfolded enzymes, and GroEL and GroES, which promote their proper folding
overexpression of holo-enzyme in Pichia pastoris strain GS115, subcloning in Escherichia coli strain DH5alpha
-
Pichia pastoris GS115 transformed using the pPICBO derivative linearized with Bpu1102I
-
recombinant expression in Pichia pastoris