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Literature summary extracted from

  • Sobolewska-Stawiarz, A.; Leferink, N.G.; Fisher, K.; Heyes, D.J.; Hay, S.; Rigby, S.E.; Scrutton, N.S.
    Energy landscapes and catalysis in nitric-oxide synthase (2014), J. Biol. Chem., 289, 11725-11738 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.14.13.39 Calmodulin in the neuronal enzyme, protein domain dynamics and calmodulin binding are implicated in regulating electron flow from NADPH, through the FAD and FMN cofactors, to the heme oxygenase domain, the site of NO generation. Binding of NADPH and calmodulin influence interdomain distance relationships as well as reaction chemistry. An important effect of calmodulin binding is to suppress adventitious electron transfer from nNOS to molecular oxygen and thereby preventing accumulation of reactive oxygen species Rattus norvegicus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.39 native rat neuronal NOS reductase domain (nNOSred) and the R1400E variant are expressed from plasmid pCRNNR in Escherichia coli BL21(DE3) Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.39 Rattus norvegicus P29476
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.39 native rat neuronal NOS reductase domain (nNOSred) and the R1400E variant Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.13.39 neuron
-
 Rattus norvegicus
-

Synonyms

EC Number Synonyms Comment Organism
1.14.13.39 NO synthase
-
 Rattus norvegicus
1.14.13.39 NOS
-
 Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.39 FAD in the neuronal enzyme, protein domain dynamics and calmodulin binding are implicated in regulating electron flow from NADPH, through the FAD and FMN cofactors, to the heme oxygenase domain, the site of NO generation Rattus norvegicus
1.14.13.39 FMN in the neuronal enzyme, protein domain dynamics and calmodulin binding are implicated in regulating electron flow from NADPH, through the FAD and FMN cofactors, to the heme oxygenase domain, the site of NO generation Rattus norvegicus
1.14.13.39 NADPH in the neuronal enzyme, protein domain dynamics and calmodulin binding are implicated in regulating electron flow from NADPH, through the FAD and FMN cofactors, to the heme oxygenase domain, the site of NO generation. Binding of NADPH and calmodulin influence interdomain distance relationships as well as reaction chemistry Rattus norvegicus