Submit Data |  Help |  Video Tutorials |  News |  Publications |  FTP Download |  REST API |  Citing RGD |  Contact   

Role of Asp1393 in catalysis, flavin reduction, NADP(H) binding, FAD thermodynamics, and regulation of the nNOS flavoprotein.

Authors: Konas, DW  Takaya, N  Sharma, M  Stuehr, DJ 
Citation: Konas DW, etal., Biochemistry. 2006 Oct 17;45(41):12596-609.
Pubmed: (View Article at PubMed) PMID:17029414
DOI: Full-text: DOI:10.1021/bi061011t

Nitric oxide synthases (NOS) are flavoheme enzymes with important roles in biology. The reductase domain of neuronal NOS (nNOSr) contains a widely conserved acidic residue (Asp(1393)) that is thought to facilitate hydride transfer between NADPH and FAD. Previously we found that the D1393V and D1393N mutations lowered the NO synthesis activity and the rates of heme and flavin reduction in full-length nNOS. To examine the mechanisms for these results in greater detail, we incorporated D1393V and D1393N substitutions into nNOSr along with a truncated NADPH-FAD domain construct (FNR) and characterized the mutants. D1393V nNOSr had markedly lower (


Gene Ontology Annotations
Objects Annotated

Additional Information

RGD Object Information
RGD ID: 1598372
Created: 2006-11-20
Species: All species
Last Modified: 2006-11-20
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.