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Literature summary for 1.1.5.4 extracted from

  • Igeno, M.; Becerra, G.; Guijo, M.; Merchan, F.; Blasco, R.
    Metabolic adaptation of Pseudomonas pseudoalcaligenes CECT5344 to cyanide: role of malate-quinone oxidoreductases, aconitase and fumarase isoenzymes (2011), Biochem. Soc. Trans., 39, 1849-1853.
    View publication on PubMed
Search for more literature for 1.1.5.4

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-malate + a quinone Pseudomonas oleovorans
-
 oxaloacetate + a quinol
-
 ?
(S)-malate + a quinone Pseudomonas oleovorans CECT 5344
-
 oxaloacetate + a quinol
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas oleovorans
-
 several mqo genes
-
Pseudomonas oleovorans CECT 5344
-
 several mqo genes
-

Source Tissue

Source Tissue Comment Organism Textmining
additional information effect of the carbon source in the growth of Pseudomonas pseudoalcaligenes CECT5344 with cyanide as a nitrogen source compared to ammonium, overview. Strain CECT5344 requires an additional carbon source for assimilating cyanide as a nitrogen source Pseudomonas oleovorans
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + a quinone
-
 Pseudomonas oleovorans oxaloacetate + a quinol
-
 ?
(S)-malate + a quinone
-
 Pseudomonas oleovorans CECT 5344 oxaloacetate + a quinol
-
 ?

Synonyms

Synonyms Comment Organism
malate-quinone oxidoreductase
-
 Pseudomonas oleovorans
Mqo
-
 Pseudomonas oleovorans

General Information

General Information Comment Organism
physiological function the enzyme is involved in cyanide degradation in association with the cyanide-insensitive electron-transfer chain Pseudomonas oleovorans