BRENDA - Enzyme Database
show all sequences of 7.1.1.5

Transient-state reduction and steady-state kinetic studies of menaquinol oxidase from Bacillus subtilis, cytochrome aa3-600 nm. Spectroscopic characterization of the steady-state species

Mattatall, N.R.; Cameron, L.M.; Hill, B.C.; Biochemistry 40, 13331-13341 (2001)

Data extracted from this reference:

KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.3
-
2,3-dimethyl-1,4-naphthoquinone
in phosphate buffer, pH 6.5, containing 0.5 mg/ml lauryl maltoside, temperature not specified in the publication
Bacillus subtilis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
copper
cytochrome aa3-600 contains CuB
Bacillus subtilis
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
-
-
Purification (Commentary)
Commentary
Organism
Ni2+-chelating-Sepharose column chromatography
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 2,3-dimethyl-1,4-naphthoquinol + O2 + n H+[side 1]
-
714146
Bacillus subtilis
2 2,3-dimethyl-1,4-naphthoquinone + 2 H2O + n H+[side 2]
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
65
-
2,3-dimethyl-1,4-naphthoquinone
in phosphate buffer, pH 6.5, containing 0.5 mg/ml lauryl maltoside, temperature not specified in the publication
Bacillus subtilis
Cofactor
Cofactor
Commentary
Organism
Structure
heme
cytochrome aa3-600 contains cytochrome a and cytochrome a3
Bacillus subtilis
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
heme
cytochrome aa3-600 contains cytochrome a and cytochrome a3
Bacillus subtilis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.3
-
2,3-dimethyl-1,4-naphthoquinone
in phosphate buffer, pH 6.5, containing 0.5 mg/ml lauryl maltoside, temperature not specified in the publication
Bacillus subtilis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
copper
cytochrome aa3-600 contains CuB
Bacillus subtilis
Purification (Commentary) (protein specific)
Commentary
Organism
Ni2+-chelating-Sepharose column chromatography
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2 2,3-dimethyl-1,4-naphthoquinol + O2 + n H+[side 1]
-
714146
Bacillus subtilis
2 2,3-dimethyl-1,4-naphthoquinone + 2 H2O + n H+[side 2]
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
65
-
2,3-dimethyl-1,4-naphthoquinone
in phosphate buffer, pH 6.5, containing 0.5 mg/ml lauryl maltoside, temperature not specified in the publication
Bacillus subtilis
Other publictions for EC 7.1.1.5
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)
749930
Pankratova
Extracellular electron transf ...
Enterococcus faecalis
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57
4597-4603
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-
-
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1
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1
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1
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1
1
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742646
Corbett
Listeria monocytogenes has bo ...
Listeria monocytogenes
Infect. Immun.
85
e00354-17
2017
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1
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5
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1
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1
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1
1
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749594
Moosa
Susceptibility of Mycobacteri ...
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1
1
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750736
Corbett
Listeria monocytogenes has bo ...
Listeria monocytogenes EGD, Listeria monocytogenes EGD ATCC BAA-679
Infect. Immun.
85
e00354
2017
-
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6
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1
1
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752258
Safarian
Structure of a bd oxidase ind ...
Geobacillus thermodenitrificans, Geobacillus thermodenitrificans NG80-2
Science
352
583-586
2016
-
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-
1
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2
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1
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1
1
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741917
Yi
Plasticity in the high affini ...
Bacillus subtilis 1A1, Bacillus subtilis
Biochemistry
54
5030-5044
2015
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1
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1
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2
1
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2
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5
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4
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2
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1
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1
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4
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2
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741850
Bossis
Prediction of high- and low-a ...
Bacillus subtilis
Biochem. J.
461
305-314
2014
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1
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5
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1
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715507
Yi
Characterization of the semiqu ...
Bacillus subtilis
J. Biol. Chem.
285
18241-18251
2010
-
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1
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1
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1
-
3
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1
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2
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1
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1
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1
1
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1
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1
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2
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1
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726366
Moebius
Heme biosynthesis is coupled t ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
107
10436-10441
2010
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1
1
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714146
Mattatall
Transient-state reduction and ...
Bacillus subtilis
Biochemistry
40
13331-13341
2001
-
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1
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1
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3
-
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1
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1
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715344
Winstedt
Enterococcus faecalis V583 con ...
Enterococcus faecalis
J. Bacteriol.
182
3863-3866
2000
-
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1
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1
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4
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715345
Winstedt
Terminal oxidases of Bacillus ...
Bacillus subtilis, Bacillus subtilis 168
J. Bacteriol.
182
6557-6564
2000
-
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1
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88
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1
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713980
Lemma
Properties of the menaquinol o ...
Bacillus subtilis, Bacillus subtilis W23
Arch. Microbiol.
163
432-438
1995
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5
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3
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9
2
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8
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1
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8
1
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1
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1
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5
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3
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9
2
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1
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8
1
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714287
Powers
Structure of the binuclear hem ...
Bacillus subtilis
Biochim. Biophys. Acta
1183
504-512
1994
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2
1
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713979
Lemma
The menaquinol oxidase of Baci ...
Bacillus subtilis, Bacillus subtilis W23
Arch. Microbiol.
159
574-578
1993
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1
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8
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11
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1
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1
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1
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1
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2
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1
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2
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11
-
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1
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715416
Lauraeus
The terminal quinol oxidases o ...
Bacillus subtilis 168, Bacillus subtilis
J. Biol. Chem.
268
11470-11473
1993
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1
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1
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89
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4
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1
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1
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4
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1
1
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