Information on EC 1.3.3.5 - bilirubin oxidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
1.3.3.5
-
RECOMMENDED NAME
GeneOntology No.
bilirubin oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 bilirubin + O2 = 2 biliverdin + 2 H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Porphyrin and chlorophyll metabolism
-
-
Biosynthesis of secondary metabolites
-
-
SYSTEMATIC NAME
IUBMB Comments
bilirubin:oxygen oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
80619-01-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
Q65MU7
UniProt
Manually annotated by BRENDA team
IFO 9531, low activity
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
IFO 9950, low activity
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(4E,15Z)-cyclobilirubin + O2
?
show the reaction diagram
-
phosphate buffer, pH 3.5-7.4
-
-
?
(4Z,15E)-cyclobilirubin + O2
?
show the reaction diagram
-
no activity above pH 4.5 in phosphate buffer
-
-
?
(4Z,15Z)-cyclobilirubin + O2
?
show the reaction diagram
-
no activity above pH 5.5 in phosphate buffer, no acticvity in citrate-lactate buffer, pH 3.7
-
-
?
1,1'-dimethylferrocene + O2
1,1'-dimethylferricenium + H2O
show the reaction diagram
-
1,1'-dimethylferrocene soluble as an inclusion complex with 2-hydroxypropyl-beta-cyclodextrin
-
?
1,3-dihydroxynaphthalene + O2
?
show the reaction diagram
-
-
-
-
?
1,5-dihydroxynaphthalene + O2
?
show the reaction diagram
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
show the reaction diagram
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
show the reaction diagram
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonate) + O2
?
show the reaction diagram
2,2'-azino-di-[3-ethylbenzthiazoline-6-sulfonic acid] + O2
?
show the reaction diagram
2,6-dimethoxyphenol + O2
? + H2O
show the reaction diagram
ascorbic acid + O2
?
show the reaction diagram
bilirubin + O2
biliverdin + H2O
show the reaction diagram
bilirubin ditaurine + O2
?
show the reaction diagram
-
-
-
-
?
biliverdin + O2
?
show the reaction diagram
catechol + O2
?
show the reaction diagram
-
67% of activity with bilirubin
-
-
?
chlorophyllin + O2
?
show the reaction diagram
-
50% of activity with bilirubin
-
-
?
cytochrome c + O2
?
show the reaction diagram
-
BOD efficiently accepts cytochrome c as an electron donor in both cases when cytochrome c is in solution or electrostatically adsorbed
-
-
?
ditaurobilirubin + O2
?
show the reaction diagram
Fe(CN)64- + O2
Fe(CN)63- + H2O
show the reaction diagram
-
-
-
-
?
ferricyanide + O2
? + H2O
show the reaction diagram
-
-
-
-
ferrocene + O2
ferricinium + H2O
show the reaction diagram
-
low activity
-
?
ferrocyanide + O2
?
show the reaction diagram
-
-
-
-
?
hemin + O2
?
show the reaction diagram
-
10% of activity with bilirubin
-
-
?
hexacyanoferrate(II) + O2
hexacyanoferrate(III) + H2O
show the reaction diagram
-
-
-
-
?
hydroquinone + O2
?
show the reaction diagram
-
20% of activity with bilirubin
-
-
?
indigo carmine + O2
?
show the reaction diagram
-
dye decolorization reaction
-
-
?
K4[Fe(CN)6] + O2
K3[Fe(CN)6] + H2O
show the reaction diagram
-
-
-
-
?
N,N-dimethyl-p-phenylenediamine + O2
?
show the reaction diagram
o-aminophenol + O2
?
show the reaction diagram
octacyanotungstate(IV) + O2
octacyanotungstate(V) + H2O
show the reaction diagram
-
-
-
-
?
p-phenylenediamine + O2
?
show the reaction diagram
pyrogallol + O2
?
show the reaction diagram
-
10% of activity with bilirubin
-
-
?
Remazol Brilliant Blue R + O2
?
show the reaction diagram
syringaldazine + O2
?
show the reaction diagram
-
-
-
-
?
[Fe(CN)6]4- + H+ + O2
[Fe(CN)6]3- + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 bilirubin + O2
2 biliverdin + 2 H2O
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
ferrocyanide is an effective electron donor to type 1 Cu2+
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu
-
contains T1 and T2/T3 redox copper centers
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
albumin
-
Antimycin
-
-
bilirubin
-
0.09 mM, complete inhibition of enzyme activity in 50 : 50 chloroform-n-heptane two-phase system
bromosulphothalein
-
1 mM, 60% inhibition
chloride
-
might inhibit the enzyme
cysteine
-
1 mM, 40% inhibition
Digitonin
-
0.1%, 50% inhibition
dithiothreitol
-
1 mM, 60% inhibition
Fe2+
-
1 mM, complete inhibition
guanidinium hydrochloride
-
reversible inactivation at 1 M, pH 7.0, kinetics, overview
hydrogen peroxide
-
-
KCl
-
50 mM, 40% inhibition
L-cysteine
-
87% inhibition at 1 mM, no significant effect at 0.1 mM
mercaptoethanol
-
1 mM, 50% inhibition
MgCl2
-
50 mM, 52% inhibition
NaN3
-
76% inhibition at 10 mM
Remazol Brilliant Blue R
-
substrate inhibition above 100 mg/l
rotenone
-
-
Sodium azide
-
0.1 mM, 42% inhibition
sodium taurocholate
-
0.5%, 50% inhibition
Thiourea
-
0.1 mM, 15% inhibition
Urate
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
-
i.e. ABTS, can serve as an electron mediator to facilitate the oxidation of remazol brilliant blue R
Salt
-
maximum activity at a ionic strength of 60 mM, independent of salt type
Triton X-100
-
0.01%, 25% increase in activity
additional information
-
the enzyme needs to be fully reduced before it gets activated for catalysis
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.032 - 0.124
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
0.076
2,2'-azino-bis(3-ethylbenzthioline-6-sulfonic acid)
-
at pH 2.7, Km increases with pH
0.25 - 0.34
2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)
0.216 - 0.822
2,6-dimethoxyphenol
0.008 - 24.22
bilirubin
0.18
Biliverdin
-
-
0.015 - 0.37
ditaurobilirubin
0.0192 - 5.966
K4[Fe(CN)6]
9.6 - 9.8
p-phenylenediamine
0.047
syringaldazine
-
at pH 8.2, lower Km at pH 7.0 and pH 9.0
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
322 - 716
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
7.17
2,2'-azino-bis(3-ethylbenzthioline-6-sulfonic acid)
-
at pH 5.3, about 3fold higher value at pH 2.5
115 - 164
2,2'-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid)
29 - 100
2,6-dimethoxyphenol
0.00133 - 583
bilirubin
20
Biliverdin
-
-
94.3 - 233
ditaurobilirubin
374 - 1259
K4[Fe(CN)6]
60 - 90
p-phenylenediamine
0.0133 - 2.08
syringaldazine
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
104.3 - 9800
bilirubin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00041
-
mutant enzyme M467L, using bilirubin as a substrate
0.00047
-
mutant enzyme N459A/M467F, using bilirubin as a substrate
0.00051
-
enzyme activity in small intestine
0.00064
-
mutant enzyme M467F, using bilirubin as a substrate
0.00157
-
enzyme activity in liver mitochondria
0.074
-
M467G mutant enzyme
0.3
-
ferrocyanide oxidase activity of mutant M467G
1.19
-
mutant enzyme M467Q, using bilirubin as a substrate
1.2
-
bilirubin oxidase activity of mutant D105A
1.67
-
mutant I402G
5.5
-
mutant 1Ru-C457S
6.42
-
mutant 2Ru-C457S
8.03
-
enzyme immobilized on alginate-silicate beads
11
-
bilirubin oxidase activity of mutant D105E
25.4
-
purified enzyme with substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), pH 6.0, 24°C
30
-
authentic enzyme
46.1
-
recombinant wild type enzyme, using bilirubin as a substrate
214.3
-
purified enzyme after anion exchange chromatography step, pH 7.5, 25°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.7
-
oxidation of 2,2'-azino-bis(3-ethylbenzthioline-6-sulfonic acid)
4
-
using 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate
4 - 7
-
assay at
4
-
optimal for ditaurobilirubin oxidation
4 - 6
-
assay at
4.2 - 7.2
-
assay at
4.5
-
for the indigo carmine dye decolorization reaction
5
-
with substrate remazol brilliant blue R, in absence of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
5 - 7
-
oxidation of 1,1'-dimethylferrocene, activity decreases above pH 7.5
6.5 - 7.5
-
using p-phenylenediamine as a substrate
7
BODs display a high activity and stability at neutral pH
8 - 8.5
-
using o-aminophenol as a substrate
8.6
-
Tris-HCl buffer
8.9 - 9.2
-
diethylethanolamine buffer
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 9.5
-
activity range, inactive above and below. In reaction with electron donor substrates, the enzyme exhibits the maximal activity at acidic pH values: pH 4.0 for 2,2'-azino-bis-[3-ethylbenzthiazoline-6-sulfonic acid] (ABTS) and pH 3.0 for potassium ferricyanide. Catalytic activity decreases on pH increase, and the enzyme becomes completely inactive at pH above 9.5. At neutral pH values, bilirubin oxidase retains about 50% maximal activity in oxidation of both substrates. In reaction with a hydrogen atom donor (catechol), the pH profile of the enzyme activity is shifted to alkaline values: enzymatic activity is not exhibited at pH below 6.0. This is probably related with the higher reactivity of the substrate as a phenolate anion
3.5 - 4.5
-
using 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as a substrate
4.5 - 8.2
-
under acidic condition enzyme oxidizes only conjugated bilirubin
5 - 8.5
-
activity range with substrate remazol brilliant blue R, profile overview
6.5 - 8
-
using p-phenylenediamine or o-aminophenol as a substrate
8 - 10
-
at pH 8.0 and 10.0: about 30% of maximum activity
additional information
-
inactive at pH 9.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24
-
assay at, substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)
28
-
using Remazol Brilliant Blue R as subsrate
30 - 60
55
-
enzyme immobilized on alginate-silicate beads
additional information
-
assay with substrate syringaldazine at 25°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 70
-
10°C: about 36% of maximum, 70°C: about 10% of maximum
20 - 60
21 - 37
-
at 24°C approximately 50% of the CotA protein is detected in the soluble fraction
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
Myrothecium verrucaria;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
x * 35000, folded enzyme, SDS-PAGE, x * 60000-65000, heat denatured, unfolded enzyme, SDS-PAGE, x * 61006, mass spectrometry
49000
-
x * 49000, recombinant glycoslated enzyme, SDS-PAGE, x * 63975, mature protein, after N-terminal cleavage, sequence determination
52000
-
gel filtration
59950
-
deduced from amino acid sequence
61006
-
x * 35000, folded enzyme, SDS-PAGE, x * 60000-65000, heat denatured, unfolded enzyme, SDS-PAGE, x * 61006, mass spectrometry
62000
-
SDS-PAGE
63975
-
x * 49000, recombinant glycoslated enzyme, SDS-PAGE, x * 63975, mature protein, after N-terminal cleavage, sequence determination
64000
-
1 * 64000, difference to deduced MW may be due to glycosylation, SDS-PAGE
68100
-
1 * 68100, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, 0.003 ml of 9.2 mg/ml protein in 10 mM Tris-HCl, pH 8.0, are mixed with 0.003 ml of recipitant solution containing 10% 2-methyl-2,4-pentanediol, 1.44 M ammonium sulfate, 10% glycerol and 0.5 M KCl, equilibration against 0.2-1.0 ml precipitant solution at 20°C, X-ray diffraction structure determination and analysis at 2.3-2.5 A resolution, modelling
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.7 - 9
-
-
391031
5 - 9.7
-
37°C, 60 min
391019
5
-
purified enzyme immobilized on a mesoporous carbon cryogel electrode displays high stability in solution at pH 5.0 and 50°C
744777
7
BODs display a high activity and stability at neutral pH
724076
8
-
stability drops when 100 mM cetyltrimethyl ammonium bromide are added to the aqueous solution, half-life of inactivation: 1500 min
391027
9
-
loss of 50% of its activity at pH 9.0
746191
9.2 - 9.7
11
-
enzyme is completey inactivated above pH 11.0 due to unfolding
391030
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4
-
pH 7.4, half-life: 300 h
20 - 30
-
at pH 2.7
20 - 60
20 - 70
-
at pH 9.0
22
-
pH 7.4, half-life: 25 h
40 - 50
-
the enzyme activity is stable after incubation for 1 h at a temperature up to 40°C, thermal stability is decreased beyond 50?C
40 - 61
-
sol-gel encapsulated BOD shows no decrease in relative activity until over 50°C while free enzyme loses some 40% activity at 40°C
50 - 70
-
the half life of BOD at 50°C is 114 min, residual activity after 30 min at 50°C is 83.3% of the original activity, at 70°C BOD activity disappears within several min
50
-
purified enzyme immobilized on a mesoporous carbon cryogel electrode displays high stability in solution at pH 5.0 and 50°C
65
-
stable for 60 min
84
-
stable for 30 min
100
-
5 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after an incubation of 8 days at physiological conditions, the enzyme loses 15% of its activity
-
bilirubin oxidase-coated carbon cathode operates for more than 1 week at 37°C in a glucose-containing physiological buffer solution. The cathode is short-lived in serum, losing its electrocatalytic activity in a few hours, caused by a product of the reaction of urate and dissolved oxygen. Exclusion of urate, by application of Nafion(TM) film in the cathode, improves the stability in serum
-
BOD can undergo non-catalytic direct electron transfer between enzyme and carbon electrode and retains its catalytic activity, 1%-2% of the immobilized BOD (as a first monolayer on the electrode surface) participates in direct electrical communication with a carbon electrode
-
immobilized enzyme, increased heat stability
-
multi-walled carbon nanotube modification of glassy carbon electrodes strongly enhances the oxygen reduction of bilirubin oxidase compared to unmodified electrodes, the quasi-reversible redox reaction might be attributed to the trinuclear T2/T3 cluster of BOD, a BOD-multi-walled carbon nanotube-modified electrode retains 70% of the initial activity for oxygen reduction after 4 days
-
the recombinant enzyme shows high tolerance towards urea
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chloroform
n-heptane
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C
4°C, 50 mM phosphate buffer, pH 7.4, less than 10% activity are lost after 2 days
-
5°C, pH 9.2-9.7, 5 d
-
freeze-dried, rehydrated at 15°C in the presence of trehalose, 20% loss of activity
-
immobilized enzyme, 4°C or 25°, stable for at least 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, charcoal, Sephadex a-50, Sephadex G-100
-
by gel filtration
DEAE-Sepharose Fast Flow column chromatography and Sephadex G-100 gel filtration
-
extracellular enzyme 3.92fold by ammonium sulfate fractionation and anion exchange chromatography, an additional step of gel filtration lowers the enzyme purity and amount
-
native enzyme by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
native enzyme by anion exchange chromatography and hydrophobic interaction chromatography
-
recombinant enzyme
-
recombinant His-tagged enzyme from Escherichia coli strain Origami B (DE3) by nickel affinity chromatography and dialysis
-
recombinant holo-enzyme from Pichia pastoris strain GS115 to homogeneity by hydrophobic interaction chromatography
-
recombinant wild-type enzyme and mutants
-
the commercial preparation of bilirubin oxidase from Myrothecium verrucaria is additionally purified by anion exchange chromatography
-
to homogeneity
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 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 Aspergillus oryzae; expression of H94V, H134/136V, C457V, C457A and H456/458V mutants in Aspergillus oryzae
-
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
-
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
bilirubin oxidase has been found to be the best enzyme for converting O2 to H2O as a cathodic enzyme in biofuel cells
C457A
-
no oxidase activity
C457S
-
can react with dioxygen, affords reaction intermediate I with absorption maxima at 340, 470, and 675 nm
C457V
-
no oxidase activity
D105A
-
exhibits 7.5% bilirubin oxidase activity compared to the wild-type enzyme, indicating that Asp105 conserved in all multi-copper oxidases donates a proton to reaction intermediates I and II
D105E
-
exhibits 46% bilirubin oxidase activity compared to the wild-type enzyme, indicating that Asp105 conserved in all multi-copper oxidases donates a proton to reaction intermediates I and II
D105N
-
does not react with dioxygen
E463Q
-
site-directed mutagenesis
H134/136V
-
no oxidase activity
H456/458V
-
no oxidase activity
H456D/H458D
-
mutant with weak bilirubin oxidase and ferroxidase activity
H456K/H458K
-
mutant with weak bilirubin oxidase and ferroxidase activity
H456V/H458V
-
inactive mutant
H94V
-
no oxidase activity
M467F
-
the mutated type I Cu center shows characteristics of phytocyanins
M467L
-
the mutated type I Cu center shows characteristics of phytocyanins
M467Q
-
the enzymatic activity of the mutant is very low toward bilirubin but it works as a good catalyst in direct electron transfer-type bioelectrocatalytic reduction of dioxygen into water, the kcat value is 3fold increased
Met467Q
-
reduced activity
N459A/M467F
-
activity is decreased to 1% of the recombinant wild type enzyme, the mutated type I Cu center shows characteristics of phytocyanins, blue copper proteins with an axial coordination of Gln, due to compensatory binding of the distal Asn459
C457S
-
virtually no enzyme activity, Ru-incorporation conferrs higher enzyme activity
I402G
-
low enzyme activity
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
biotechnology
diagnostics
energy production
-
the BOD from Bacillus pumilus is an attractive candidate for application in biofuel cells and biosensors showing high activity at neutral pH and high tolerance towards NaCl
environmental protection
industry
medicine
synthesis
additional information
Show AA Sequence (138 entries)
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