Competition involving biogenic NO.
This review considers competitive reactions of NO biosynthesis and its interaction with its targets including enzyme competition for arginine, competition between the substrates in the NO-synthase active sites, competitive sources of arginine, multiple states of NO-synthases resulting from competition of reducible cofactors (FAD, FMN, BH4, heme), competition between aqueous and lipophilic phases for NO resulting in efficient micellar catalysis, and other aspects of competition involving biogenic NO.
Nedospasov
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Institute of Molecular Genetics, Russian Academy of Sciences, Moscow, 123182, Russia. nedospas@img.ras.ru
D000818:Animals; D001120:Arginine / Q000378:metabolism; D001667:Binding, Competitive; D020134:Catalytic Domain; D006801:Humans; D007700:Kinetics; D009249:NADP / Q000378:metabolism; D009569:Nitric Oxide / Q000096:biosynthesis*; D019001:Nitric Oxide Synthase / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity
D009569:Nitric Oxide; D009249:NADP; D001120:Arginine; D019001:Nitric Oxide Synthase