Information on EC 1.10.3.13 - caldariellaquinol oxidase (H+-transporting)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.10.3.13
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RECOMMENDED NAME
GeneOntology No.
caldariellaquinol oxidase (H+-transporting)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 caldariellaquinol + O2 + n H+[side 1] = 2 caldariellaquinone + 2 H2O + n H+[side 2]
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
biosynthesis of special quinones
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SYSTEMATIC NAME
IUBMB Comments
caldariellaquinol:O2 oxidoreductase (H+-transporting)
A copper-containing cytochrome. The enzyme from thermophilic archaea is part of the terminal oxidase and catalyses the reduction of O2 to water, accompanied by the extrusion of protons across the cytoplasmic membrane.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768
the enzyme may be involved in the electron pathway, it may be involved in regulatory adaptation to environmental stress
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 caldariellaquinol + O2 + n H+[side 1]
2 caldariellaquinone + 2 H2O + n H+[side 2]
show the reaction diagram
2,3,5,6-tetrachlorobenzoquinol + oxidized dithiothreitol
?
show the reaction diagram
-
-
-
-
?
4 ferrocytochrome c + O2 + 4 H+
4 ferricytochrome c + 2 H2O
show the reaction diagram
caldariella quinol + O2 + n H+/in
caldariella quinone + H2O + n H+/out
show the reaction diagram
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
show the reaction diagram
menadiol + oxidized dithiothreitol
menadione + dithiothreitol
show the reaction diagram
-
-
-
-
?
N,N,N',N'-tetramethyl-1,4-phenylenediamine + O2
?
show the reaction diagram
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N,N,N',N'-tetramethyl-1,4-phenylenediamine-ascorbate dependent oxygen consumption
-
-
?
N,N,N',N'-tetramethyl-1,4-phenylenediamine + O2 + n H+/in
?
show the reaction diagram
P39480 and P98004 and P39479 and P39477
the SoxABCD complex is a proton-pumping quinol oxidase. With N,N,N',N'-tetramethyl-1,4-phenylenediamine as a reductant, the SoxABCD complex reconstituted into liposomes generates a proton motive force. The purified SoxABCD oxidase does not react with cytochrome c or blue copper proteins such as halocyanine or azurin as electron donors. However, considerable turnover numbers are found with N,N,N',N'-tetramethyl-1,4-phenylenediamine or caldariellaquinol, confirming that in vivo the enzyme is acting as a quinol oxidase
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-
?
N,N,N',N'-tetramethyl-1,4-phenylenediamine + oxidized dithiothreitol
?
show the reaction diagram
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the physiological electron donor of the SoxABCD complex is probably caldariellaquinol. Since caldariellaquinol is very hydrophobic and difficult to use in vitro, N,N,N',N'-tetramethyl-1,4-phenylenediamine is used as a convenient artificial substrate
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-
?
N,N,N',N'-tetramethyl-1,4-phenylenediamine hydrochloride + O2
?
show the reaction diagram
additional information
?
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starting with the ascorbate plus N,N,N’,N'-tetramethyl-p-phenylendiamine-reduced enzyme, intramolecular electron transfer within this complex is very rapid
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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
caldariella quinol + O2 + n H+/in
caldariella quinone + H2O + n H+/out
show the reaction diagram
P94117 and P94118
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-
-
?
caldariellaquinol + O2 + n H+/in
caldariellaquinone + H2O + n H+/out
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome
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the active respiratory terminal oxidase segment of Sulfolobus sp. strain 7 contains one non-CO-reactive b-type cytochrome (b562) and two different a-type cytochromes (a583 and aa3), in addition to one copper and a Rieske-type FeS cluster, which, as a whole, function as an active caldariellaquinol oxidase supercomplex
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
Fe
P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768
the enzyme contains a total of seven metal redox centers. One of it, the blue copper protein sulfocyanin, functionally links two subcomplexes. One is a bb3-type terminal oxidase moiety containing CuA and CuB, whereas the other consists of a Rieske FeS-protein and a homolog to cytochrome b – in this case hosting two hemes AS. Based on a 1:1 stoichiometry, 1 mol complex contains 6 mol Fe and 4 mol Cu
Iron
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heme-copper enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-decylchinolone
P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768
pI50: 4.9
2-dodecyl-N-hydroxychinolone
P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768
pI50: 5.9
2-methyl-3-dodecyl-N-hydroxy-chinolone
P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768
pI50: 7.3
2-methyl-3-dodecylchinolone
P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768
pI50: 6.2
3-methyl-2-decylchinolone
P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768
pI50: 5.5
azide
Cl-
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70 mM, 50% inhibition
cyanide
EDTA
P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768
causes maximal inhibition of either the isolated enzyme, or the activity of the crude membrane extract by 63% with a half-maximal effect at 21 mM
ferrocytochrome c
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0.002 mM, 50% inhibition of N,N,N',N'-tetramethyl-1,4-phenylenediamine-ascorbate dependent oxygen consumption
KCN
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1 mM, 76% inhibition
NaN3
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1 mM, 76% inhibition
phosphate
SO42-
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28 mM, 50% inhibition
Sulfide
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1-3 mM, complete inhibition
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026 - 0.036
caldariellaquinol
0.057
ferrocytochrome c
P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768
pH 4.5, 50°C
0.23
menadiol
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pH 6. 40°C
0.046 - 0.333
N,N,N',N'-tetramethyl-1,4-phenylenediamine
0.1
N,N,N',N'-tetramethyl-1,4-phenylenediamine hydrochloride
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pH 7.0, 40°C
0.032
O2
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pH 7.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
239 - 393
caldariellaquinol
1.5
ferrocytochrome c
Aeropyrum pernix
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pH 7.5, 40°C
66.9 - 404
N,N,N',N'-tetramethyl-1,4-phenylenediamine
additional information
additional information
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9200 - 11000
caldariellaquinol
4655
2300 - 8700
N,N,N',N'-tetramethyl-1,4-phenylenediamine
6155
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.9
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pH 6, 40°C, oxidation of N,N,N',N'-tetramethyl-1,4-phenylenediamine
36
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pH 7.0, 40°C, oxidation of N,N,N',N'-tetramethyl-1,4-phenylenediamine hydrochloride
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768
assay at
5.3
P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768
assay at
80
high thermostability of the soluble form of subunit SoxH
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11000
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x * 47000 + x * 19000 + x * 11000, the enzyme is composed of at least three polypeptides, SDS-PAGE
18900
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x * 18900 (SoxA) + x * 58000 (SoxB) + x * 62600 (SoxC) + SoxD + ?. The SoxABCD quinol oxidase complex contains at least five different polypeptides. In addition to the major subunits SoxA, SoxB and SoxC, it has two small polypeptides. One of these is the translation product of a short open reading frame (called the soxD gene) at the end of the operon
19000
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x * 47000 + x * 19000 + x * 11000, the enzyme is composed of at least three polypeptides, SDS-PAGE
20000
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x * 40000 + x * 27000 + x * 20000, SDS-PAGE
27000
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x * 40000 + x * 27000 + x * 20000, SDS-PAGE
38000
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x * 38000
40000
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x * 40000 + x * 27000 + x * 20000, SDS-PAGE
47000
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x * 47000 + x * 19000 + x * 11000, the enzyme is composed of at least three polypeptides, SDS-PAGE
58000
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x * 18900 (SoxA) + x * 58000 (SoxB) + x * 62600 (SoxC) + SoxD + ?. The SoxABCD quinol oxidase complex contains at least five different polypeptides. In addition to the major subunits SoxA, SoxB and SoxC, it has two small polypeptides. One of these is the translation product of a short open reading frame (called the soxD gene) at the end of the operon
62600
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x * 18900 (SoxA) + x * 58000 (SoxB) + x * 62600 (SoxC) + SoxD + ?. The SoxABCD quinol oxidase complex contains at least five different polypeptides. In addition to the major subunits SoxA, SoxB and SoxC, it has two small polypeptides. One of these is the translation product of a short open reading frame (called the soxD gene) at the end of the operon
87082
x * 87082, calulated from sequence
100000 - 104000
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gel filtration
149000
P94117 and P94118
assuming a 1:1 stoichiometry of all encoded subunits, the Acidianus ambivalens aa3-type quinol oxidase represents a complex with a calculated molecular mass of 149000 Da. Subunits doxA and doxB later classified as EC 1.8.5.2, thiosulfate dehydrogenase (quinone)
224000
P39481 and Q97UN3 and Q53765 and Q53766 and Q59825 and Q53768
gel filtration
280000
570000
P39480 and P98004 and P39479 and P39477
when membrane solubilization is carried out at low salt concentration, an oligomeric state of the oxidase is obtained
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant expression of sulfocyanin
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
SoxM is expressed under heterotrophic growth conditions