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Enzyme Nomenclature
Information on EC 1.10.3.12 - menaquinol oxidase (H+-transporting)
for references in articles please use BRENDA:EC1.10.3.12
Word Map on EC 1.10.3.12
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
1.10.3.12
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RECOMMENDED NAME
GeneOntology No.
menaquinol oxidase (H+-transporting)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 menaquinol + O2 = 2 menaquinone + 2 H2O
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-
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SYSTEMATIC NAME
IUBMB Comments
menaquinol:O2 oxidoreductase (H+-transporting)
Cytochrome aa3-600, one of the principal respiratory oxidases from Bacillus subtilis, is a member of the heme-copper superfamily of oxygen reductases, and is a close homologue of the cytochrome bo3 ubiquinol oxidase from Escherichia coli, but uses menaquinol instead of ubiquinol as a substrate.The enzyme also pumps protons across the membrane bilayer, generating a proton motive force.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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the FMN enzyme protoporphyrinogen IX oxidase (HemG) of Escherichia coli abstracts six electrons from its substrate and transfers them via ubiquinone, cytochrome bo3 and cytochrome bd oxidase to oxygen. Under anaerobic conditions electrons are transferred via menaquinone, fumarate and nitrate reductase. Cyo, Cyd and Nar contribute to the proton motive force that drives ATP formation. oxygen-dependent cytochrome oxidases, cytochrome bo3 (Cyo) and cytochrome bd (Cyd) oxidase, sustain up to 67% (Cyd) and 78% (Cyo) of HemG activity in the absence of ubiquinone, indicating a tight association of the quinones with the enzyme complexes during preparation
physiological function
physiological function
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cytochrome aa3 is the most important terminal oxidase contributing to proton motive force generation in exponentially growing cells
physiological function
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cytochrome aas-600 is the major terminal oxidase in lopgh ase cells
physiological function
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the enzyme is important during murine infection
physiological function
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cytochrome aa3 is the most important terminal oxidase contributing to proton motive force generation in exponentially growing cells; cytochrome aas-600 is the major terminal oxidase in lopgh ase cells
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3-dimethyl-1,4-naphthoquinone + O2
2,3-dimethyl-1,4-naphthoquinol + H2O
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-
-
-
?
2,3-dimethyl-1,4-naphthoquinol + O2
2,3-dimethyl-1,4-naphthoquinone + H2O
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best substrate
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-
?
2,3-dimethyl-1,4-naphthoquinol + O2
2,3-dimethyl-1,4-naphthoquinone + H2O
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best substrate
-
-
?
menaquinol + O2
menaquinone + H2O
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cyt aa3-600 is strictly a menaquinol oxidase
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-
?
additional information
?
-
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cytochrome aa3-600 is a proton-pumping terminal oxidase
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-
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additional information
?
-
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no activity with 1,4-naphthoquinol, N,N,N',N'-tetramethyl-1,4-phenylenediamine plus ascorbate or reduced cytochrome c
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-
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additional information
?
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the enzyme does not oxidize 1,4-naphthoquinol, 2,3-dimethoxy-5-methyl-6-(n-nonyl)-1,4-benzoquinol, and 2,3-dimethoxy-5-methyl- 1,4-benzoquinol
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-
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additional information
?
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cytochrome aa3-600 is a proton-pumping terminal oxidase
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-
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additional information
?
-
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the enzyme does not oxidize 1,4-naphthoquinol, 2,3-dimethoxy-5-methyl-6-(n-nonyl)-1,4-benzoquinol, and 2,3-dimethoxy-5-methyl- 1,4-benzoquinol
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additional information
?
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no activity with 1,4-naphthoquinol, N,N,N',N'-tetramethyl-1,4-phenylenediamine plus ascorbate or reduced cytochrome c
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
menaquinol + O2
menaquinone + H2O
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cyt aa3-600 is strictly a menaquinol oxidase
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome
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the isolated enzyme contains 0.0053 mM cytochrome aa 3 per gram of protein and negligible amounts of cytochrome b and c
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cytochrome
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the enzyme contains 7 mol cytochrome aa 3 per g protein which corresponds to 2 mol heme A per mol enzyme
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heme
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cytochrome aa3-600 is a member of the heme-copper superfamily of oxygen reductases
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
Cu2+
copper
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the enzyme contains a binuclear heme iron-copper site with only one copper CuB, while the Cu A center is lacking
Cu2+
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cytochrome aa3-600 is a member of the heme-copper superfamily of oxygen reductases
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
antimycin A
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more than 10fold less effective than 2-(n-heptyl)-4-hydroxyquinoline-N-oxide, 39% residual activity at 0.01 mM
Myxothiazol
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more than 10fold less effective than 2-(n-heptyl)-4-hydroxyquinoline-N-oxide, 45% residual activity at 0.01 mM
Stigmatellin
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more than 10fold less effective than 2-(n-heptyl)-4-hydroxyquinoline-N-oxide, 39% residual activity at 0.01 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
2,3-dimethyl-1,4-naphthoquinone
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in phosphate buffer, pH 6.5, containing 0.5 mg/ml lauryl maltoside, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
65
2,3-dimethyl-1,4-naphthoquinone
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in phosphate buffer, pH 6.5, containing 0.5 mg/ml lauryl maltoside, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13686
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
15000
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1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
20000
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1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
22670
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
33640
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
36000
54000
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1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
57000
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the preparation consists of two major (57000 Da and 36000 Da) polypeptides
73834
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA
36000
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the preparation consists of two major (57000 Da and 36000 Da) polypeptides
36000
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1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
heterotetramer
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA; 1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
heterotetramer
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1 * 33640 + 1 * 73834 + 1 * 22670 + 1 * 13686, subunits QoxA, QoxB, QoxC and QoxD, calculated from sequence of cDNA; 1 * 36000 + 1 * 54000 + 1 * 20000 + 1 * 15000, subunits QoxA, QoxB, QoxC and QoxD, SDS-PAGE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography, 1.25 equivalents of menaquinone-7 co-purify with the enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Bacillus subtilis strain LUW143 lacking both the aa3-600 menaquinol oxidase and caa3-type cytochrome c oxidase
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
R70H
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LINKS TO OTHER DATABASES (specific for EC-Number 1.10.3.12)
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