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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.39 bacterial NOS, phylogenetic tree, functional expression in Escherichia coli Bacillus subtilis
1.14.13.39 bacterial NOS, phylogenetic tree, functional expression in Escherichia coli Bacillus anthracis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.39 additional information Bacillus subtilis the bacterial enzyme, bNOS, lacks an essential reductase domain, that supplies electrons during NO biosynthesis, and is thus limited with respect to a pool of available redox partners, but does produce NO in living cells and accomplish this task by hijacking available cellular redox partners that are not normally committed to NO production, bacterial reductase also supports NO synthesis by the oxygenase domain of mammalian NOS expressed in Escherichia coli, overview ?
-
 ?
1.14.13.39 additional information Bacillus anthracis the bacterial enzyme, bNOS, lacks an essential reductase domain, that supplies electrons during NO biosynthesis, and is thus limited with respect to a pool of available redox partners, but does produce NO in living cells and accomplish this task by hijacking available cellular redox partners that are not normally committed to NO production, bacterial reductase also supports NO synthesis by the oxygenase domain of mammalian NOS expressed in Escherichia coli, overview ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.39 Bacillus anthracis
-
-
-
1.14.13.39 Bacillus subtilis
-
-
-
1.14.14.47 Bacillus anthracis
-
-
-
1.14.14.47 Bacillus subtilis
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.13.39 additional information
-
-
 Bacillus subtilis
1.14.13.39 additional information
-
-
 Bacillus anthracis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.39 additional information the bacterial enzyme, bNOS, lacks an essential reductase domain, that supplies electrons during NO biosynthesis, and is thus limited with respect to a pool of available redox partners, but does produce NO in living cells and accomplish this task by hijacking available cellular redox partners that are not normally committed to NO production, bacterial reductase also supports NO synthesis by the oxygenase domain of mammalian NOS expressed in Escherichia coli, overview Bacillus subtilis ?
-
 ?
1.14.13.39 additional information the bacterial enzyme, bNOS, lacks an essential reductase domain, that supplies electrons during NO biosynthesis, and is thus limited with respect to a pool of available redox partners, but does produce NO in living cells and accomplish this task by hijacking available cellular redox partners that are not normally committed to NO production, bacterial reductase also supports NO synthesis by the oxygenase domain of mammalian NOS expressed in Escherichia coli, overview Bacillus anthracis ?
-
 ?
1.14.14.47 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 ?
1.14.14.47 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

EC Number Synonyms Comment Organism
1.14.13.39 bacterial nitric-oxide synthase
-
 Bacillus subtilis
1.14.13.39 bacterial nitric-oxide synthase
-
 Bacillus anthracis
1.14.13.39 bNOS
-
 Bacillus subtilis
1.14.13.39 bNOS
-
 Bacillus anthracis
1.14.14.47 bNOS
-
 Bacillus subtilis
1.14.14.47 bNOS
-
 Bacillus anthracis

General Information

EC Number General Information Comment Organism
1.14.14.47 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
1.14.14.47 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