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Literature summary for 1.14.14.47 extracted from

  • Gusarov, I.; Starodubtseva, M.; Wang, Z.Q.; McQuade, L.; Lippard, S.J.; Stuehr, D.J.; Nudler, E.
    Bacterial nitric-oxide synthases operate without a dedicated redox partner (2008), J. Biol. Chem., 283, 13140-13147.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Bacillus anthracis
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-
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Bacillus subtilis
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 L-arginine + 3 reduced flavodoxin + 4 O2
-
Bacillus subtilis 2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O flavodoxins YkuN and YkuP as well as protein cisJ may be used as redox partners, enzyme uses different available cellular redox partner to support its NO synthesis ?
2 L-arginine + 3 reduced flavodoxin + 4 O2
-
Bacillus anthracis 2 L-citrulline + 2 nitric oxide + 3 oxidized flavodoxin + 4 H2O flavodoxins YkuN and YkuP as well as protein cisJ may be used as redox partners, enzyme uses different available cellular redox partner to support its NO synthesis ?

Synonyms

Synonyms Comment Organism
bNOS
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Bacillus subtilis
bNOS
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Bacillus anthracis

General Information

General Information Comment Organism
physiological function enzyme activity is important for maintaining normal growth at the log-to-stationary transition phase. Enzyme produces NO in living cells and uses available cellular redox partners that are not normally committed to NO production. The promiscuous bacterial reductase also supports NO synthesis by the oxygenase domain of mammalian nitric oxide synthase expressed in Escherichia coli Bacillus subtilis
physiological function enzyme activity is important for maintaining normal growth at the log-to-stationary transition phase. Enzyme produces NO in living cells and uses available cellular redox partners that are not normally committed to NO production. The promiscuous bacterial reductase also supports NO synthesis by the oxygenase domain of mammalian nitric oxide synthase expressed in Escherichia coli Bacillus anthracis