BRENDA - Enzyme Database show
show all sequences of 1.2.2.4

Three mammalian cytochromes b561 are ascorbate-dependent ferrireductases

Su, D.; Asard, H.; FEBS J. 273, 3722-3734 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression and activity assay in Saccharomyces cerevisiae S288C deltafre1 deltafre2. The strain is deficient of ferrireductases. Chromaffin granule cytochrome b-561 could partially restore the wild-type phenotype; expression and activity assay in Saccharomyces cerevisiae S288C deltafre1 deltafre2. The strain is deficient of ferrireductases. Duodenal cytochrome b-561 could partially restore the wild-type phenotype; expression and activity assay in Saccharomyces cerevisiae S288C deltafre1 deltafre2. The strain is deficient of ferrireductases. Lysosomal cytochrome b-561 could partially restore the wild-type phenotype
Mus musculus
Engineering
Amino acid exchange
Commentary
Organism
D38A
similar to wild-type, mutation in the transmembrane domain
Mus musculus
E177A
similar to wild-type, mutation in the electron donating site
Mus musculus
E196A
23% activity, mutation in the electron donating site
Mus musculus
F44A
45% activity, mutation in the transmembrane domain
Mus musculus
H105A
similar to wild-type, mutation in the electron donating site
Mus musculus
H112A
similar to wild-type, mutation in the electron donating site
Mus musculus
H117A
inactive, residues involved in heme-binding
Mus musculus
H156A
inactive, residues involved in heme-binding
Mus musculus
H47A
inactive, residues involved in heme-binding
Mus musculus
H83A
inactive, residues involved in heme-binding
Mus musculus
M51A
similar to wild-type, mutation in the transmembrane domain
Mus musculus
N106A
similar to wild-type, mutation in the electron donating site
Mus musculus
P48A
similar to wild-type, mutation in the transmembrane domain
Mus musculus
Q131A
45% activity, mutation in the transmembrane domain
Mus musculus
R149A
25% activity, residue at the electron-accepting site of the protein
Mus musculus
R67A
incative, domain predicted to bind ascorbate at the electron-accepting site of the protein
Mus musculus
S115A
50% activity, mutation in the electron donating site
Mus musculus
S118A
similar to wild-type, mutation in the electron donating site
Mus musculus
W119A
17% activity, mutation in the electron donating site
Mus musculus
Y190A
similar to wild-type, mutation in the electron donating site
Mus musculus
Y66A
incative, domain predicted to bind ascorbate at the electron-accepting site of the protein
Mus musculus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
27000
-
deduced from sequence, Western blot
Mus musculus
27800
-
deduced from sequence, Western blot
Mus musculus
31500
-
deduced from sequence, Western blot
Mus musculus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
-
-
-
Mus musculus
-
-
-
Rattus norvegicus
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell culture
-
Mus musculus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Fe3+-EDTA + H2O + ferrocytochrome b-561
-
673552
Mus musculus
Fe2+-EDTA + H+ + ferricytochrome b-561
-
-
-
?
potassium ferricyanide + H2O + ferrocytochrome b-561
-
673552
Mus musculus
potassium ferrocyanide + H+ + ferricytochrome b-561
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
ascorbate
-
Mus musculus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression and activity assay in Saccharomyces cerevisiae S288C deltafre1 deltafre2. The strain is deficient of ferrireductases. Chromaffin granule cytochrome b-561 could partially restore the wild-type phenotype; expression and activity assay in Saccharomyces cerevisiae S288C deltafre1 deltafre2. The strain is deficient of ferrireductases. Duodenal cytochrome b-561 could partially restore the wild-type phenotype; expression and activity assay in Saccharomyces cerevisiae S288C deltafre1 deltafre2. The strain is deficient of ferrireductases. Lysosomal cytochrome b-561 could partially restore the wild-type phenotype
Mus musculus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ascorbate
-
Mus musculus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D38A
similar to wild-type, mutation in the transmembrane domain
Mus musculus
E177A
similar to wild-type, mutation in the electron donating site
Mus musculus
E196A
23% activity, mutation in the electron donating site
Mus musculus
F44A
45% activity, mutation in the transmembrane domain
Mus musculus
H105A
similar to wild-type, mutation in the electron donating site
Mus musculus
H112A
similar to wild-type, mutation in the electron donating site
Mus musculus
H117A
inactive, residues involved in heme-binding
Mus musculus
H156A
inactive, residues involved in heme-binding
Mus musculus
H47A
inactive, residues involved in heme-binding
Mus musculus
H83A
inactive, residues involved in heme-binding
Mus musculus
M51A
similar to wild-type, mutation in the transmembrane domain
Mus musculus
N106A
similar to wild-type, mutation in the electron donating site
Mus musculus
P48A
similar to wild-type, mutation in the transmembrane domain
Mus musculus
Q131A
45% activity, mutation in the transmembrane domain
Mus musculus
R149A
25% activity, residue at the electron-accepting site of the protein
Mus musculus
R67A
incative, domain predicted to bind ascorbate at the electron-accepting site of the protein
Mus musculus
S115A
50% activity, mutation in the electron donating site
Mus musculus
S118A
similar to wild-type, mutation in the electron donating site
Mus musculus
W119A
17% activity, mutation in the electron donating site
Mus musculus
Y190A
similar to wild-type, mutation in the electron donating site
Mus musculus
Y66A
incative, domain predicted to bind ascorbate at the electron-accepting site of the protein
Mus musculus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
27000
-
deduced from sequence, Western blot
Mus musculus
27800
-
deduced from sequence, Western blot
Mus musculus
31500
-
deduced from sequence, Western blot
Mus musculus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cell culture
-
Mus musculus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Fe3+-EDTA + H2O + ferrocytochrome b-561
-
673552
Mus musculus
Fe2+-EDTA + H+ + ferricytochrome b-561
-
-
-
?
potassium ferricyanide + H2O + ferrocytochrome b-561
-
673552
Mus musculus
potassium ferrocyanide + H+ + ferricytochrome b-561
-
-
-
?
Other publictions for EC 1.2.2.4
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
698576
Swingley
The complete genome sequence o ...
Roseobacter denitrificans OCh 114
J. Bacteriol.
189
683-690
2007
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
673552
Su
Three mammalian cytochromes b5 ...
Homo sapiens, Mus musculus, Rattus norvegicus
FEBS J.
273
3722-3734
2006
-
-
1
-
21
-
-
-
-
-
3
-
-
3
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
21
-
-
-
-
-
-
-
3
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
656481
Hanzelmann
The effect of intracellular mo ...
Hydrogenophaga pseudoflava
J. Mol. Biol.
301
1221-1235
2000
-
-
-
-
-
-
-
-
2
1
-
-
-
4
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390482
Dobbek
Crystal structure and mechanis ...
Oligotropha carboxidovorans
Proc. Natl. Acad. Sci. USA
96
8884-8889
1999
-
-
-
1
-
-
-
-
-
-
3
-
-
4
-
1
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390483
Kang
Cloning and molecular characte ...
Hydrogenophaga pseudoflava
J. Bacteriol.
181
5581-5590
1999
-
-
1
-
-
-
-
-
-
2
3
-
-
2
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
2
3
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
655594
Hanzelmann
-
The redox centers in the molyb ...
Pseudomonas thermocarboxydovorans
FEMS Microbiol. Lett.
176
139-145
1999
-
-
-
-
-
-
-
-
-
2
2
-
-
1
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
2
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
11606
Jacobitz
Removal of CO dehydrogenase fr ...
Oligotropha carboxidovorans
J. Bacteriol.
171
6294-6299
1989
-
-
-
-
-
-
-
-
3
1
-
-
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
11607
Meyer
-
Biochemistry, and physiology o ...
Hydrogenibacillus schlegelii, Hydrogenophaga pseudoflava, Oligotropha carboxidovorans, Pseudomonas carboxydohydrogena, Pseudomonas thermocarboxydovorans
FEMS Microbiol. Rev.
39
161-179
1986
-
-
-
-
-
-
-
2
2
9
14
5
-
5
-
-
-
-
-
-
-
-
10
3
-
-
-
-
-
-
-
8
-
-
-
-
-
-
8
-
-
-
-
-
-
2
2
9
14
5
-
-
-
-
-
-
-
-
10
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-