Mutation of Glu-361 in human endothelial nitric-oxide synthase selectively abolishes L-arginine binding without perturbing the behavior of heme and other redox centers

Journal of Biological Chemistry

Volumn 272, Issue 10, 1997, Pages 6114-6118

  Chen, Pei Feng ^a   Tsai, Ah Lim ^a   Berka, Vladimir ^a   Wu, Kenneth K ^a  

^a UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; HEME; MUTANT PROTEIN; NITRIC OXIDE SYNTHASE;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; ENDOTHELIUM; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME BINDING; HUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ARGININE; BINDING SITES; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENDOTHELIUM, VASCULAR; GLUTAMATES; HEME; HEMEPROTEINS; HUMANS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; NADP; NITRIC OXIDE SYNTHASE; OXIDATION-REDUCTION; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0030889046     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.10.6114     Document Type: Article

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