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Literature summary extracted from

  • Kabashima, Y.; Sone, N.; Kusumoto, T.; Sakamoto, J.
    Purification and characterization of malate:quinone oxidoreductase from thermophilic Bacillus sp. PS3 (2013), J. Bioenerg. Biomembr., 45, 131-136.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.5.4 DNA and amino acid sequence determination and analysis, phylogenetic analysis Bacillus sp. (in: Bacteria)

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.5.4 CoCl2 79% inhibition at 1 mM Bacillus sp. (in: Bacteria)
1.1.5.4 CuCl2 completely inhibits the enzyme at 0.01 mM Bacillus sp. (in: Bacteria)
1.1.5.4 CuSO4 completely inhibits the enzyme at 0.1 mM Bacillus sp. (in: Bacteria)
1.1.5.4 MnCl2 86% inhibition at 1 mM Bacillus sp. (in: Bacteria)
1.1.5.4 additional information o-phenanthroline does not significantly affect activity Bacillus sp. (in: Bacteria)
1.1.5.4 NaN3 65% inhibition at 1 mM Bacillus sp. (in: Bacteria)
1.1.5.4 NiSO4 67% inhibition at 1 mM Bacillus sp. (in: Bacteria)
1.1.5.4 pyridoxal 5'-phosphate 28% inhibition at 1 mM Bacillus sp. (in: Bacteria)

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.5.4 50000
-
2 * 50000, about, SDS-PAGE Bacillus sp. (in: Bacteria)
1.1.5.4 92000
-
gel filtration Bacillus sp. (in: Bacteria)

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.5.4 (S)-malate + quinone Bacillus sp. (in: Bacteria)
-
oxaloacetate + quinol
-
?
1.1.5.4 (S)-malate + quinone Bacillus sp. (in: Bacteria) PS3
-
oxaloacetate + quinol
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.4 Bacillus sp. (in: Bacteria)
-
-
-
1.1.5.4 Bacillus sp. (in: Bacteria) PS3
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.4 (S)-malate + dimethyl naphthoquinone
-
Bacillus sp. (in: Bacteria) oxaloacetate + dimethyl naphthoquinol
-
?
1.1.5.4 (S)-malate + dimethyl naphthoquinone
-
Bacillus sp. (in: Bacteria) PS3 oxaloacetate + dimethyl naphthoquinol
-
?
1.1.5.4 (S)-malate + duroquinone
-
Bacillus sp. (in: Bacteria) oxaloacetate + duroquinol
-
?
1.1.5.4 (S)-malate + duroquinone
-
Bacillus sp. (in: Bacteria) PS3 oxaloacetate + duroquinol
-
?
1.1.5.4 (S)-malate + menaquinone-1 menadione as the direct electron acceptor and dichloroindophenol, DCIP, as the final electron-acceptor Bacillus sp. (in: Bacteria) oxaloacetate + menaquinol-1
-
?
1.1.5.4 (S)-malate + quinone
-
Bacillus sp. (in: Bacteria) oxaloacetate + quinol
-
?
1.1.5.4 (S)-malate + quinone
-
Bacillus sp. (in: Bacteria) PS3 oxaloacetate + quinol
-
?
1.1.5.4 (S)-malate + ubiquinone
-
Bacillus sp. (in: Bacteria) oxaloacetate + ubiquinol
-
?
1.1.5.4 (S)-malate + ubiquinone
-
Bacillus sp. (in: Bacteria) PS3 oxaloacetate + ubiquinol
-
?
1.1.5.4 additional information the enzyme shows specificity towards ubiquinone, duroquinone, and dimethyl naphthoquinone in addition to menaquinone. And the enzyme also shows malate dehydrogenase activity, EC 1.1.1.37, overview Bacillus sp. (in: Bacteria) ?
-
?
1.1.5.4 additional information the enzyme shows specificity towards ubiquinone, duroquinone, and dimethyl naphthoquinone in addition to menaquinone. And the enzyme also shows malate dehydrogenase activity, EC 1.1.1.37, overview Bacillus sp. (in: Bacteria) PS3 ?
-
?

Subunits

EC Number Subunits Comment Organism
1.1.5.4 dimer 2 * 50000, about, SDS-PAGE Bacillus sp. (in: Bacteria)

Synonyms

EC Number Synonyms Comment Organism
1.1.5.4 malate:quinine oxidoreductase
-
Bacillus sp. (in: Bacteria)
1.1.5.4 menaquinone reductase
-
Bacillus sp. (in: Bacteria)
1.1.5.4 Mqo
-
Bacillus sp. (in: Bacteria)

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.5.4 45
-
-
Bacillus sp. (in: Bacteria)

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.5.4 7.5
-
-
Bacillus sp. (in: Bacteria)

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.4 FAD noncovalently bound as a prosthetic group Bacillus sp. (in: Bacteria)
1.1.5.4 menaquinone
-
Bacillus sp. (in: Bacteria)
1.1.5.4 additional information the enzymeis active with duroquinone and dimethyl naphthoquinone Bacillus sp. (in: Bacteria)
1.1.5.4 ubiquinone
-
Bacillus sp. (in: Bacteria)

General Information

EC Number General Information Comment Organism
1.1.5.4 additional information because of the differences in the redox potentials of NAD+ and quinones, the MQO-catalyzed reaction progresses spontaneously compared to the MDH-catalyzed reaction, EC 1.1.1.37 Bacillus sp. (in: Bacteria)