Mutation of conserved tryptophan residues at the dimer interface of Staphylococcus aureus nitric oxide synthase

► Staphylococcus aureus NOS was mutated at invariant residues W314 and W316. ► Position-314 mutants have lower substrate affinity, but can still dimerize. ► Position-316 mutants resembled wild type, but with lower activity. ► The orientation of W314 may be a conformational switch to control activity...

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Veröffentlicht in:	Archives of biochemistry and biophysics 2011-02, Vol.506 (2), p.165-172
Hauptverfasser:	Lustig, Daniel Ben, Kempt, Cora, Alam, Samiah, Clancy, James, Yee, Janet, Rafferty, Steven Patrick
Format:	Artikel
Sprache:	eng
Schlagworte:	alanine Amino Acid Substitution arginine Arginine - metabolism Bacterial nitric oxide synthase Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Catalytic Domain Conserved Sequence Dimerization Enzyme Activation enzyme activity heme Hemeprotein histidine hydrogen bonding Kinetics Models, Molecular Mutagenesis Mutagenesis, Site-Directed mutation nitric oxide synthase Nitric Oxide Synthase - chemistry Nitric Oxide Synthase - genetics Nitric Oxide Synthase - metabolism oxidation phenylalanine polypeptides Protein Interaction Domains and Motifs Protein Structure, Quaternary proteins Pterin Quaternary structure Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Spectrophotometry Staphylococcus aureus Staphylococcus aureus - enzymology Staphylococcus aureus - genetics Substrate Specificity temperature tryptophan Tryptophan - chemistry tyrosine
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