Literature summary for 1.14.13.39 extracted from

Li, W.; Fan, W.; Chen, L.; Elmore, B.O.; Piazza, M.; Guillemette, J.G.; Feng, C.
Role of an isoform-specific serine residue in FMN-heme electron transfer in inducible nitric oxide synthase (2012), J. Biol. Inorg. Chem., 17, 675-685.

Search for more literature for 1.14.13.39

Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C563R	interdomain electron transfer rate is similar to that of the wildtype	Homo sapiens
R536E	mutant constructed to disrupt the bridging calmodulin/nitric oxide synthase interaction. The FMN-heme interdomain electron transfer rate is decreased by 96%	Homo sapiens
S562K	inducible nitric oxide synthase mutant in an oxygenase/FMN construct. The interdomain electron transfer rate constant of the mutant is decreased by one third, and its flavin fluorescence intensity per micromole per liter is diminished by approximately 24% suggesting that a positive charge at position 562 destabilizes the hydrogen-bond-mediated nitric oxide synthase/calmodulin alignment, resulting in slower FMN-heme interdomain electron transfer	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P35228	isoform Nos2, inducible nitric oxide synthase	-

Synonyms

Synonyms	Comment	Organism
NOS2	-	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)