Species: Pseudomonas putida No. 352
Subunit composition of theobromine demethylase = [theobromine demethylase subunit]6
The native apparent molecular mass was determined by gel filtration chromatography [Asano94].
Cloning of the gene encoding this enzyme has not been reported.
This monooxygenase was shown to be specific for theobromine demethylation at the N3 position to produce 7-methylxanthine. Based on its absorption at 415 nm and brown color in solution, it was suggested to contain either heme or nonheme iron. Pseudomonas putida No. 352 also showed high caffeine degradation activity when grown in the presence of Fe3+ [Asano94].
A soluble, NADH-dependent caffeine demethylating monooxygenase activity was also found in extracts of this organism and the formation of formaldehyde was demonstrated. In contrast to this enzyme, the caffeine demethylase activity was not inhibited by Zn2+ [Asano94].
The subunit apparent molecular mass was determined by SDS-PAGE [Asano94].
Molecular Weight of Polypeptide: 41.0 kD (experimental) [Asano94 ]
Molecular Weight of Multimer: 250.0 kD (experimental) [Asano94]
Enzymatic reaction of: theobromine N3-demethylase (theobromine demethylase)
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is physiologically favored in the direction shown.
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