Nitric oxide synthases: Domain structure and alignment in enzyme function and control

Frontiers in Bioscience

Volumn , Issue 4, 2003, Pages

  Ghosh, Dipak K ^a   Salerno, J C ^b,c  

^a DUKE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b Research Rensselaer Polytechnic Institute   (United States)

^c RENSSELAER POLYTECHNIC INSTITUTE   (United States)

Author keywords

Arginine analogs; Domain alignment; EPR; Flavoprotein reductase CaM; H4 biopterin; Nitric oxide; NO synthase; NO synthase Inhibitors; Review; Structure function; X ray structure

Indexed keywords

ARGININE; CALMODULIN; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; OXIDOREDUCTASE; OXYGENASE;

AMINO ACID SEQUENCE; BINDING SITE; CATALYSIS; CRYSTAL STRUCTURE; CYTOTOXICITY; DIMERIZATION; ELECTRON TRANSPORT; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; ENZYME REGULATION; ENZYME STRUCTURE; EVOLUTION; GENE FUSION; HUMAN; IMMUNE RESPONSE; NONHUMAN; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; REVIEW; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS; ANIMAL; CHEMISTRY; PHYSIOLOGY; PROTEIN FOLDING; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION;

EUKARYOTA; PROKARYOTA;

ANIMALS; HUMANS; NITRIC OXIDE SYNTHASE; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0043154640     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/959     Document Type: Review

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