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Literature summary extracted from

  • Luebben, M.; Warne, A.; Albracht, S.P.; Saraste, M.
    The purified SoxABCD quinol oxidase complex of Sulfolobus acidocaldarius contains a novel haem (1994), Mol. Microbiol., 13, 327-335.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.1.1.4 azide 0.2 mM, complete inhibition Sulfolobus acidocaldarius
7.1.1.4 additional information no inhibition by myxothiazol, antimycin, funiculosin, 2-heptyl-4-hydroxyquinoline-N-oxide, 5-n-undecyl-6-hydroxy-2,7-dioxobenzothiazole and 3-(3,4-dichlorophenyl)-1,3-dimethylurea Sulfolobus acidocaldarius

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.1.1.4 0.07
-
N,N,N',N'-tetramethyl-1,4-phenylenediamine pH 6. 40°C Sulfolobus acidocaldarius
7.1.1.4 0.23
-
menadiol pH 6. 40°C Sulfolobus acidocaldarius

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.1.1.4 membrane
-
Sulfolobus acidocaldarius 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
7.1.1.4 18900
-
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 Sulfolobus acidocaldarius
7.1.1.4 58000
-
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 Sulfolobus acidocaldarius
7.1.1.4 62600
-
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 Sulfolobus acidocaldarius
7.1.1.4 280000
-
detergent-SoxABCD protein complex, gel filtration Sulfolobus acidocaldarius

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.1.1.4 caldariellaquinol + O2 + n H+/in Sulfolobus acidocaldarius 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 an artificial substrate caldariellaquinone + H2O + n H+/out
-
?

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.4 Sulfolobus acidocaldarius
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.1.1.4
-
Sulfolobus acidocaldarius

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.1.1.4 9.9
-
pH 6, 40°C, oxidation of N,N,N',N'-tetramethyl-1,4-phenylenediamine Sulfolobus acidocaldarius

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.4 2,3,5,6-tetrachlorobenzoquinol + oxidized dithiothreitol
-
Sulfolobus acidocaldarius ?
-
?
7.1.1.4 caldariellaquinol + O2 + n H+/in 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 an artificial substrate Sulfolobus acidocaldarius caldariellaquinone + H2O + n H+/out
-
?
7.1.1.4 menadiol + oxidized dithiothreitol
-
Sulfolobus acidocaldarius menadione + dithiothreitol
-
?
7.1.1.4 N,N,N',N'-tetramethyl-1,4-phenylenediamine + oxidized dithiothreitol 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 Sulfolobus acidocaldarius ?
-
?

Subunits

EC Number Subunits Comment Organism
7.1.1.4 ? 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 Sulfolobus acidocaldarius

Synonyms

EC Number Synonyms Comment Organism
7.1.1.4 SoxABCD quinol oxidase
-
Sulfolobus acidocaldarius

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
7.1.1.4 40
-
assay at Sulfolobus acidocaldarius

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7.1.1.4 additional information
-
additional information menadiol and 2,3,5,6-tetrachlorobenzoquinol show turnover numbers of 30-40 e-/s. The highest activity of 100 e-/s can be obtained with N,N,N',N'-tetramethyl-1,4-phenylenediamine Sulfolobus acidocaldarius

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.1.1.4 6
-
assay at Sulfolobus acidocaldarius

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.4 heme the SoxABCD quinol oxidase complex probably contains four A-type hemes which are bound to SoxB and SoxC. The structure of these hemes is not identical to heme A. The Sulfolobus heme As has a 2-hydroxyethyl geranylgeranyl in position 2 of the porphyrin ring whereas heme A has the related farnesyl-containing side-chain Sulfolobus acidocaldarius