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Literature summary for 1.5.1.38 extracted from

  • Gao, B.; Ellis, H.R.
    Mechanism of flavin reduction in the alkanesulfonate monooxygenase system (2007), Biochim. Biophys. Acta, 1774, 359-367.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
FMN + NADPH + H+ Escherichia coli
-
 FMNH2 + NADP+
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
FMN + NADPH + H+
-
 Escherichia coli FMNH2 + NADP+
-
 ?
FMN + NADPH + H+ results from single-wavelength analyses at 450 and 550 nm show that reduction of FMN occurs in three distinct phases. Following a possible rapid equilibrium binding of FMN and NADPH to SsuE (MC-1) that occurs before the first detectable step, an initial fast phase (241 s-1) corresponds to the interaction of NADPH with FMN (CT-1). The second phase is a slow conversion (11 s-1) to form a charge-transfer complex of reduced FMNH2 with NADP+ (CT-2), and represents electron transfer from the pyridine nucleotide to the flavin. The third step (19 s-1) is the decay of the charge-transfer complex to SsuE with bound products (MC-2) or product release from the CT-2 complex. Results from isotope studies with [(4R)-2H]NADPH demonstrates a rate-limiting step in electron transfer from NADPH to FMN Escherichia coli FMNH2 + NADP+
-
 ?

Synonyms

Synonyms Comment Organism
SsuE
-
 Escherichia coli

General Information

General Information Comment Organism
physiological function FMN reductase (SsuE) catalyzes the reduction of FMN by NADPH, and the reduced flavin is transferred to the monooxygenase (SsuD) Escherichia coli