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Rieske monooxygenase NdmA from the highly efficient caffeine-degrading strain Pseudomonas sp. NCIM 5235: Recombinant expression, characterization, and biotransformation studies

delete2026-05-05
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PRE
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P
Pranjali Singh
S
Sathyanarayana N. Gummadi*
DOI：10.1016/j.bej.2026.110238delete
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Abstract

Abstract

En 中文
• Novel N1-specific demethylase (NdmA) from Pseudomonas sp. NCIM 5235. • Exogenous metal ions increase the NdmA activity as much as Fe2+ • Reductase-NdmD required in excess for higher activity of NdmA • Cu²⁺ ions caused complete inhibition of the NdmA-NdmD enzyme system.
Keywords:
NdmA
caffeine degradation
Rieske monooxygenase
metal ions
reductase NdmD

Journal

Biochemical Engineering Journal cover
Biochemical Engineering Journal
IF:
3.8
Papers:
6.2K
Citations:
1.4W

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