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Literature summary for 1.5.1.30 extracted from

  • Kozmin, S.G.; Wang, J.; Schaaper, R.M.
    Role for CysJ flavin reductase in molybdenum cofactor-dependent resistance of Escherichia coli to 6-N-hydroxylaminopurine (2010), J. Bacteriol., 192, 2026-2033.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Synonyms

Synonyms Comment Organism
CysJ component of the CysJI sulfite reductase complex Escherichia coli
NADPH:flavin oxidoreductase
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Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Escherichia coli

General Information

General Information Comment Organism
metabolism CysJ functions as a specific partner of the YcbX molybdoenzyme and provides the reducing equivalents needed for the detoxification reaction at the YcbX molybdocenter Escherichia coli
physiological function CysJ is involved in 6-N-hydroxylaminopurine resistance Escherichia coli