Critical Role of Val567 in Substrate Recognition by Neuronal Nitric Oxide Synthase for NO Formation Activity

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Abstract Leu and Phe mutations at conserved Val567 located within the substrate binding site of neuronal nitric oxide synthase markedly lowered activity on the physiological substrates, l-Arg and NG-hydroxy-l-Arg, and other potential alkyl- and arylguanidine substrates, suggesting that the residue at this position is important for substrate recognition by the enzyme.