Title : A conserved flavin-shielding residue regulates NO synthase electron transfer and nicotinamide coenzyme specificity.

Pub. Date : 2002 Oct 15

PMID : 12359874






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Nitric oxide synthases (NOSs) are flavoheme enzymes that contain a ferredoxin:NADP(+)-reductase (FNR) module for binding NADPH and FAD and are unusual because their electron transfer reactions are controlled by the Ca(2+)-binding protein calmodulin. NADP ferredoxin reductase Homo sapiens
2 Nitric oxide synthases (NOSs) are flavoheme enzymes that contain a ferredoxin:NADP(+)-reductase (FNR) module for binding NADPH and FAD and are unusual because their electron transfer reactions are controlled by the Ca(2+)-binding protein calmodulin. NADP ferredoxin reductase Homo sapiens
3 A conserved aromatic residue in the FNR module of NOS shields the isoalloxazine ring of FAD and is known to regulate NADPH binding affinity and specificity in related flavoproteins. NADP ferredoxin reductase Homo sapiens