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Literature summary for 1.14.13.39 extracted from

  • Tiso, M.; Tejero, J.; Panda, K.; Aulak, K.S.; Stuehr, D.J.
    Versatile regulation of neuronal nitric oxide synthase by specific regions of its C-terminal tail (2007), Biochemistry, 46, 14418-14428.
    View publication on PubMed
Search for more literature for 1.14.13.39

Activating Compound

Activating Compound Comment Organism Structure
Calmodulin activates the neuronal NOS by binding and inhibiting the suppression through the C-terminal tail of the enzyme, overview Rattus norvegicus

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged wild-type enzyme and untagged truncation mutant enzyme in Escherichia coli strain BL21(DE3) Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information construction of a truncated mutant lacking the terminal half of the C-terminus, i.e. residues from Ile1413 to Ser1429. The mutation has almost no impact on NADP+ release, flavin reduction, flavin autoxidation, heme reduction, reductase activity, or NO synthesis activity, but does prevent an increase in FMN shielding that normally occurs in response to NADPH binding. Additional removal of the C-terminal alpha-helix, residues 1401 to 1412, significantly increases the NADP+ release rate, flavin autoxidation, and NADPH oxidase activity, and causes hyper-deshielding of the FMN cofactor associated with increased reductase activity and slightly diminished heme reduction and NO synthesis. Further removal of residues downstream from Gly1396, a full C-terminus truncation, amplifies the aforementioned effects and in addition altered NADP+ interaction with FAD, relieves the kinetic suppression on flavin reduction, and further diminishes heme reduction and NO synthesis Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ in the heme cofactor Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus three unique structural elements are involved in the catalytic suppression of NOS: an autoinhibitory element in the FMN binding module, a CD2A loop in the connecting subdomain, and a C-terminal extension or tail, the C-terminal tail of nNOS is a regulatory element that suppresses nNOS activities in the absence of bound calmodulin, it may help stabilize the FMN-shielded conformation by holding the FMN module up against the FNR module as required for inter-flavin electron transfer, mechanism, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant truncation mutant from Escherichia coli strain BL21(DE3) by sequential 2',5'-ADP and calmodulin affinity chromatography Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
brain nNOS Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information three unique structural elements are involved in the catalytic suppression of NOS: an autoinhibitory element in the FMN binding module, a CD2A loop in the connecting subdomain, and a C-terminal extension or tail, the C-terminal tail of nNOS is a regulatory element that suppresses nNOS activities in the absence of bound calmodulin, it may help stabilize the FMN-shielded conformation by holding the FMN module up against the FNR module as required for inter-flavin electron transfer, mechanism, overview Rattus norvegicus ?
-
 ?
additional information the reduced recombinant trunaction mutant nNOSr performs autooxidation in presence of NADPH, interactions, overview Rattus norvegicus ?
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 ?

Subunits

Subunits Comment Organism
More nNOS reductase structure homology modeling, overview Rattus norvegicus

Synonyms

Synonyms Comment Organism
neuronal nitric oxide synthase
-
 Rattus norvegicus
nNOS
-
 Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
 assay at room temperature Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6
-
 assay at Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
FMN an inverse correlation exists between FMN shielding and the cytochrome c reductase activity Rattus norvegicus
heme an inverse correlation exists between FMN shielding and the cytochrome c reductase activity Rattus norvegicus
NADPH binding structure of NADP(H) to wild-type and truncation mutant enzyme lacking parts of the C-terminus, overview Rattus norvegicus