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Literature summary for 1.1.5.4 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)

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

Inhibitors

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + dimethyl naphthoquinone
-
Bacillus sp. (in: Bacteria) oxaloacetate + dimethyl naphthoquinol
-
?
(S)-malate + dimethyl naphthoquinone
-
Bacillus sp. (in: Bacteria) PS3 oxaloacetate + dimethyl naphthoquinol
-
?
(S)-malate + duroquinone
-
Bacillus sp. (in: Bacteria) oxaloacetate + duroquinol
-
?
(S)-malate + duroquinone
-
Bacillus sp. (in: Bacteria) PS3 oxaloacetate + duroquinol
-
?
(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
-
?
(S)-malate + quinone
-
Bacillus sp. (in: Bacteria) oxaloacetate + quinol
-
?
(S)-malate + quinone
-
Bacillus sp. (in: Bacteria) PS3 oxaloacetate + quinol
-
?
(S)-malate + ubiquinone
-
Bacillus sp. (in: Bacteria) oxaloacetate + ubiquinol
-
?
(S)-malate + ubiquinone
-
Bacillus sp. (in: Bacteria) PS3 oxaloacetate + ubiquinol
-
?
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) ?
-
?
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

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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

General Information

General Information Comment Organism
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)