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Literature summary for 4.1.2.32 extracted from

  • Boulton, C.A.; Large, P.J.
    Inactivation of trimethylamine N-oxide aldolase (demethylase) during preparation of bacterial extracts (1979), FEMS Microbiol. Lett., 5, 159-162.
No PubMed abstract available

Organism

Organism UniProt Comment Textmining
Aminobacter aminovorans
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Pseudomonas aminovorans NCIB 9039
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Purification (Commentary)

Purification (Comment) Organism
partial Aminobacter aminovorans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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specific activity is much higher in ultrasonic extracts of Pseudomonas aminovorans grown on methylamine than in cells grown on trimethylamine and trimethylamine N-oxide, low activity in trimethylamine and trimethylamine N-oxide grown cells is due to the presence of an inactivating factor. The inactivating factor is absent from methylamine-grown cells Aminobacter aminovorans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Trimethylamine N-oxide
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Aminobacter aminovorans Dimethylamine + formaldehyde
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