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Literature summary for 1.14.13.39 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
Search for more literature for 1.14.13.39

Activating Compound

Activating Compound Comment Organism Structure
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)

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P29476
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
neuron
-
 Rattus norvegicus
-

Synonyms

Synonyms Comment Organism
NO synthase
-
 Rattus norvegicus
NOS
-
 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
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
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
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